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Amino Acids, Proteins and DNA

A-Level AQA Chemistry

This pack of flashcards encompasses foundational concepts related to amino acids, proteins, and DNA, including their structures, properties, and roles in biological systems. It also covers enzyme function, drug interactions with enzymes, and the molecular details of DNA bases and nucleotides, as well as cisplatin's mechanism as an anticancer drug.

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"Define nucleotides."	"Nucleotides are composed of a phosphate ion bonded to 2-deoxyribose, which is in turn bonded to one of the four bases: adenine, cytosine, guanine, or thymine."
"What are ionic interactions in the context of protein tertiary structure?"	"Ionic interactions can form between acidic amino acids (e.g., aspartic acid) and basic amino acids (e.g., lysine) in the folded protein chain."
"Describe the formation of sulfur bridges in protein tertiary structure."	"If two cysteine side chains end up near each other due to folding, they can react to form a covalent sulfur bridge."
"What is the role of hydrogen bonds in protein tertiary structure?"	"Hydrogen bonds contribute to the stability and folding of the protein by forming interactions between different amino acid side chains."
"Define ionic interactions in the context of protein tertiary structure."	"Ionic interactions refer to the attraction between positively charged and negatively charged amino acid side chains in the folded protein chain."
"How do sulfur bridges contribute to the stability of protein tertiary structure?"	"Sulfur bridges, formed by the reaction of cysteine side chains, provide covalent bonds that help stabilize the folded protein structure."
"Describe enzymes."	"Enzymes are proteins that act as catalysts in biological reactions."
"What is the active site of an enzyme?"	"The active site of an enzyme is a hollow substrate in the globular protein structure where a substrate molecule can bind."
"How do substrate molecules bind to the active site of an enzyme?"	"Substrate molecules bind to the active site of an enzyme through a variety of interactions, including hydrogen bonding, van der Waals forces, and ionic interactions."
"Define the lock and key hypothesis."	"The lock and key hypothesis states that only substrate molecules with the right shape and correct positions of functional groups will fit and bind to the active site of an enzyme."
"Describe the role of drugs as enzyme inhibitors."	"Many drugs act as enzyme inhibitors by blocking the active site of an enzyme, preventing the substrate from attaching and inhibiting the enzyme's function."
"How can computers be used to help design drugs that act as enzyme inhibitors?"	"Computers can be used to simulate and model the interactions between drugs and enzymes, aiding in the design of drugs that specifically target and inhibit enzyme activity."
"What are some of the interactions involved in substrate binding to the active site of an enzyme?"	"Some of the interactions involved in substrate binding to the active site of an enzyme include hydrogen bonding, van der Waals forces, and ionic interactions."
"Describe the role of the active site in enzyme catalysis."	"The active site of an enzyme is where the substrate binds and undergoes a catalyzed reaction. It provides a specific environment for the reaction to occur, increasing the rate of the reaction."
"Describe the key molecules in DNA."	"The key molecules in DNA are phosphate ions, 2-deoxyribose (a pentose sugar), and the four bases: adenine, cytosine,anine, and thymine."
"How do hydrogen bonds contribute to the tertiary structure?"	"Hydrogen bonds can form between different amino acid side chains in the folded protein chain."
"How are the bases in DNA attached to the sugar?"	"The bases in DNA are attached to the sugar (2-deoxyribose) through specific atoms on the base that join onto the sugar molecule."
"What are the four bases in DNA?"	"The four bases in DNA are adenine (A), cytosine (C), guanine (G), and thymine (T)."
"Describe the structure of a nucleotide."	"A nucleotide consists of a phosphate ion bonded to 2-deoxyribose, which is further bonded to one of the four bases: adenine, cytosine, guanine, or thymine."
"Describe the structure of a single strand of DNA."	"A single strand of DNA is a sugar-phosphate polymer chain with bases attached to the sugars in the chain."
"What is the role of hydrogen bonding in DNA?"	"Hydrogen bonding between base pairs leads to the formation of the two complementary strands of DNA."
"Define complementary strands in DNA."	"Complementary strands in DNA refer to two strands that have base sequences that match, with adenine (A) pairing with thymine (T) and cytosine (C) pairing with guanine (G)."
"How do guanine and cytosine pair in DNA?"	"Guanine pairs with cytosine in DNA through three hydrogen bonds."
"Describe the structure of DNA."	"DNA exists as two complementary strands of the sugar-phosphate polymer chain arranged in the form of a double helix."
"Describe the structure of cisplatin."	"Cisplatin is a Pt(II) complex with two chloride ions and two ammonia ligands bound to a central platinum atom."
"What is the function of cisplatin as an anticancer drug?"	"Cisplatin prevents DNA replication in cancer cells by forming a dative covalent bond with a nitrogen atom on guanine."
"How does cisplatin prevent the replication of cancerous cells?"	"Cisplatin displaces two chloride ions and binds to the DNA, inhibiting replication."
"Define ligand replacement reaction."	"A ligand replacement reaction is a chemical reaction in which one ligand is replaced by another ligand in a coordination complex."
"What are the potential side effects of cisplatin?"	"Potential side effects of cisplatin include hair loss and replication inhibition in healthy cells."
"What is the purpose of wearing plastic gloves during the chromatography of amino acids?"	"Wearing plastic gloves is necessary to prevent contamination."
"What is the significance of the alpha in 'a' amino acid?"	"The alpha in 'a' amino acid means that both the NH2 and COOH groups are joined to the same carbon."
"Define optical activity in relation to amino acids."	"Optical activity refers to the ability of amino acids to rotate plane polarized light."
"What are zwitterions?"	"Zwitterions are dipolar forms of amino acids that have both a positive and negative charge."
"Describe the acidity and basicity of amino acids."	"The amine group in amino acids is basic, while the carboxylic acid group is acidic."
"What is the role of amino acids as buffers?"	"Amino acids act as weak buffers and can gradually change pH when small amounts of acid or alkali are added."
"Explain the difference between the no charge form and the dipolar zwitterion form of an amino acid."	"The no charge form of an amino acid never occurs, while the dipolar zwitterion form is the most stable and exists in solution."
"What is the effect of pH on the form of amino acids with extra carboxylic acid or amine groups?"	"In alkaline conditions, the extra carboxylic acid group will react and change form, while in acidic conditions, the extra amine group will react and change form."
"What are dipeptides?"	"Dipeptides are simple combination molecules of two amino acids with one amide (peptide) link."
"How many possible combinations of amino acids are there in a dipeptide?"	"For any two different amino acids, there are two possible combinations in a dipeptide."
"Describe the reactions that can occur with the carboxylic acid and amine groups in amino acids."	"The carboxylic acid group and amine group in amino acids can undergo the usual reactions of these functional groups, such as esterification."
"What happens when proteins are heated with concentrated hydrochloric acid or strong alkalis?"	"They can be hydrolysed and split back into their constituent amino acids."
"How can the composition of a protein molecule be deduced?"	"The composition of the protein molecule can be deduced by using TLC chromatography."
"Describe the process of splitting a protein into amino acids."	"A protein can be split into amino acids by reacting with concentrated hydrochloric acid."
"How can you ensure that the spots for each sample are equally spaced along the pencil line on the TLC plate?"	"By drawing a pencil line 1 cm above the bottom of the TLC plate and marking spots for each sample equally spaced along the line."
"Define the Rf value in chromatography."	"The Rf value is calculated by dividing the distance moved by the amino acid by the distance moved by the solvent."
"What is the purpose of spraying ninhydrin on the amino acids and heating them?"	"Spraying ninhydrin on the amino acids and heating them causes red to blue spots to appear, making the transparent amino acids visible."
"Describe the primary structure of proteins."	"The primary structure of proteins is the sequence of combinations of amino acids."
"What are proteins made from?"	"Proteins are polymers made from combinations of amino acids."
"Define peptide links."	"Peptide links are the amide functional group that join amino acids together in proteins."
"How are amino acids linked together in proteins?"	"Amino acids are linked together by condensation reactions with peptide links."
"Describe the secondary structure of proteins."	"The secondary structure of proteins can take the form of an alpha-helix or a pleated sheet structure."
"What holds the alpha-helix structure of proteins in place?"	"The alpha-helix structure of proteins is held in place by hydrogen bonds between the H of -N-H group and the -O of C=O of the fourth amino acid along the chain."
"How is the pleated sheet structure of proteins formed?"	"The pleated sheet structure of proteins is formed when the protein chain folds into parallel strands held together by hydrogen bonds between the H of -N-H group and the -O of C=O of amino acids further along the chain in the parallel region."
"What is the role of R-groups in the secondary structure of proteins?"	"The R-groups on the amino acids are all pointed to the outside of the alpha-helix structure of proteins."
"What is the tertiary structure of proteins?"	"The tertiary structure is the folding of the secondary structure into more complex shapes."
"Describe the interactions that hold the tertiary structure in place."	"The tertiary structure is held in place by interactions between the R-side groups in more distant amino acids, including hydrogen bonding, sulfur-sulfur bonds, and ionic interactions."

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Front

Define nucleotides.

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Nucleotides are composed of a phosphate ion bonded to 2-deoxyribose, which is in turn bonded to one of the four bases: adenine, cytosine, guanine, or thymine.

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This can lead to a range of effects, from slowing down specific biochemical processes to treating medical conditions.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979588,"front":"How can computers be used to help design drugs that act as enzyme inhibitors?","back":"Computers can be used to simulate and model the interactions between drugs and enzymes, aiding in the design of drugs that specifically target and inhibit enzyme activity.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":11,"explanation":"Computational methods allow researchers to visualize molecular interactions, predict binding affinities, and optimize drug structures. 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These interactions collectively contribute to the enzyme's catalytic efficiency.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979590,"front":"Describe the role of the active site in enzyme catalysis.","back":"The active site of an enzyme is where the substrate binds and undergoes a catalyzed reaction. It provides a specific environment for the reaction to occur, increasing the rate of the reaction.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":13,"explanation":"The active site is crucial for enzyme specificity, as its unique shape and chemical environment allow only certain substrates to bind. This selective interaction lowers the activation energy required for the reaction, facilitating faster product formation while ensuring that the enzyme remains unchanged after the reaction.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979591,"front":"Describe the key molecules in DNA.","back":"The key molecules in DNA are phosphate ions, 2-deoxyribose (a pentose sugar), and the four bases: adenine, cytosine,anine, and thymine.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":14,"explanation":"The key molecules in DNA are essential for its structure and function. Phosphate ions form the backbone, while 2-deoxyribose and the four bases (adenine, cytosine, guanine, and thymine) make up the nucleotides. These molecules are crucial for encoding genetic information and facilitating cellular processes.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979567,"front":"How do hydrogen bonds contribute to the tertiary structure?","back":"Hydrogen bonds can form between different amino acid side chains in the folded protein chain.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":15,"explanation":"Hydrogen bonds play a crucial role in stabilizing the tertiary structure of proteins by forming between polar groups in the amino acid side chains. These bonds help maintain the specific 3D shape of the protein, influencing its function and stability.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979593,"front":"How are the bases in DNA attached to the sugar?","back":"The bases in DNA are attached to the sugar (2-deoxyribose) through specific atoms on the base that join onto the sugar molecule.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":16,"explanation":"The bases in DNA are attached to the sugar (2-deoxyribose) through specific atoms on the base that join onto the sugar molecule. This attachment forms the backbone of the DNA molecule, creating the characteristic double helix structure. The specific bonding between the bases and the sugar is essential for the stability and function of the DNA molecule.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979594,"front":"What are the four bases in DNA?","back":"The four bases in DNA are adenine (A), cytosine (C), guanine (G), and thymine (T).","front_language":"English","back_language":"English","front_image":"","back_image":"","order":17,"explanation":"Adenine pairs with thymine, while cytosine pairs with guanine, forming the rungs of the DNA ladder. This complementary base pairing is crucial for DNA replication and the encoding of genetic information, ensuring accurate transmission of traits across generations.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979595,"front":"Describe the structure of a nucleotide.","back":"A nucleotide consists of a phosphate ion bonded to 2-deoxyribose, which is further bonded to one of the four bases: adenine, cytosine, guanine, or thymine.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":18,"explanation":"Nucleotides are the building blocks of DNA, playing a crucial role in genetic information storage. The phosphate group provides a negative charge, aiding in the formation of the DNA backbone, while the sugar and base determine the nucleotide's identity and pairing, essential for DNA replication and function.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979597,"front":"Describe the structure of a single strand of DNA.","back":"A single strand of DNA is a sugar-phosphate polymer chain with bases attached to the sugars in the chain.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":19,"explanation":"A single strand of DNA consists of nucleotides linked by covalent bonds between the sugar of one nucleotide and the phosphate group of the next. The bases (adenine, thymine, cytosine, guanine) project from the sugar, allowing for potential pairing with complementary bases in a double-stranded structure.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979599,"front":"What is the role of hydrogen bonding in DNA?","back":"Hydrogen bonding between base pairs leads to the formation of the two complementary strands of DNA.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":20,"explanation":"Hydrogen bonding in DNA is crucial for maintaining the double helix structure by binding the complementary base pairs (adenine-thymine, guanine-cytosine). This bonding is essential for DNA replication, transcription, and overall stability of the genetic code.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979600,"front":"Define complementary strands in DNA.","back":"Complementary strands in DNA refer to two strands that have base sequences that match, with adenine (A) pairing with thymine (T) and cytosine (C) pairing with guanine (G).","front_language":"English","back_language":"English","front_image":"","back_image":"","order":21,"explanation":"Complementary DNA strands are essential for DNA replication and transcription processes. The base pairing specificity ensures accurate copying of genetic information. This complementary base pairing is crucial for maintaining the genetic code and stability of DNA molecules.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979602,"front":"How do guanine and cytosine pair in DNA?","back":"Guanine pairs with cytosine in DNA through three hydrogen bonds.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":22,"explanation":"Guanine and cytosine's pairing is crucial for the stability of the DNA double helix. The three hydrogen bonds create a stronger interaction compared to adenine-thymine pairs, which only form two. This difference in bonding contributes to the overall integrity and fidelity of genetic information during replication.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979603,"front":"Describe the structure of DNA.","back":"DNA exists as two complementary strands of the sugar-phosphate polymer chain arranged in the form of a double helix.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":23,"explanation":"DNA's double helix structure is crucial for its function in storing genetic information. The complementary strands allow for accurate replication and repair, while the sugar-phosphate backbone provides stability. This arrangement also facilitates the compact packaging of DNA within the cell nucleus.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979605,"front":"Describe the structure of cisplatin.","back":"Cisplatin is a Pt(II) complex with two chloride ions and two ammonia ligands bound to a central platinum atom.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":24,"explanation":"Cisplatin's structure is a Pt(II) complex with two chloride ions and two ammonia ligands bound to a central platinum atom. This arrangement creates a square planar geometry, which is crucial for its biological activity as an anticancer agent.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979606,"front":"What is the function of cisplatin as an anticancer drug?","back":"Cisplatin prevents DNA replication in cancer cells by forming a dative covalent bond with a nitrogen atom on guanine.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":25,"explanation":"Cisplatin's anticancer function lies in its ability to hinder DNA replication in cancer cells. This is achieved through the formation of a dative covalent bond with a nitrogen atom on guanine, disrupting the cell's ability to proliferate.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979608,"front":"How does cisplatin prevent the replication of cancerous cells?","back":"Cisplatin displaces two chloride ions and binds to the DNA, inhibiting replication.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":26,"explanation":"Cisplatin's mechanism of action involves binding to DNA and disrupting its structure, which interferes with the replication process in cancerous cells. This disruption ultimately leads to cell death, making it an effective chemotherapy agent for certain types of cancer.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979609,"front":"Define ligand replacement reaction.","back":"A ligand replacement reaction is a chemical reaction in which one ligand is replaced by another ligand in a coordination complex.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":27,"explanation":"Ligand replacement reactions occur in coordination complexes when one ligand is substituted by another. This process is driven by factors such as the relative strengths of the incoming and outgoing ligands, as well as the steric and electronic properties of the complex.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979611,"front":"What are the potential side effects of cisplatin?","back":"Potential side effects of cisplatin include hair loss and replication inhibition in healthy cells.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":28,"explanation":"Cisplatin is known to cause hair loss and inhibit the replication of healthy cells, leading to potential side effects. This is due to its mechanism of action, which can affect rapidly dividing cells such as hair follicles and normal cells. These side effects are important considerations in the use of cisplatin for cancer treatment.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979553,"front":"What is the purpose of wearing plastic gloves during the chromatography of amino acids?","back":"Wearing plastic gloves is necessary to prevent contamination.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":29,"explanation":"Wearing plastic gloves is crucial in laboratory settings to maintain the integrity of samples. Contamination can alter results, leading to inaccurate data. Gloves also protect the user from potentially harmful substances, ensuring safety while handling chemicals or biological materials during experiments.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979540,"front":"What is the significance of the alpha in 'a' amino acid?","back":"The alpha in 'a' amino acid means that both the NH2 and COOH groups are joined to the same carbon.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":30,"explanation":"The alpha in 'a' amino acid is significant because it indicates the position of the amino group (NH2) and the carboxyl group (COOH) on the same carbon atom. This arrangement is crucial for the formation of peptide bonds and the structure of proteins.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979541,"front":"Define optical activity in relation to amino acids.","back":"Optical activity refers to the ability of amino acids to rotate plane polarized light.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":31,"explanation":"Optical activity is a fundamental property of chiral molecules, such as amino acids, which possess asymmetric carbon atoms. This characteristic allows them to exist in enantiomeric forms, each capable of rotating polarized light in opposite directions, influencing their biological functions and interactions in living organisms.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979542,"front":"What are zwitterions?","back":"Zwitterions are dipolar forms of amino acids that have both a positive and negative charge.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":32,"explanation":"Zwitterions play a crucial role in biochemistry, particularly in the behavior of amino acids in solution. Their unique structure allows them to interact with both polar and nonpolar environments, influencing protein folding and stability. This dual charge also affects solubility and reactivity in biological systems.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979543,"front":"Describe the acidity and basicity of amino acids.","back":"The amine group in amino acids is basic, while the carboxylic acid group is acidic.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":33,"explanation":"Amino acids contain both acidic and basic functional groups. The amine group acts as a base, accepting protons, while the carboxylic acid group acts as an acid, donating protons. This duality allows amino acids to act as both acids and bases in different chemical environments.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979544,"front":"What is the role of amino acids as buffers?","back":"Amino acids act as weak buffers and can gradually change pH when small amounts of acid or alkali are added.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":34,"explanation":"Amino acids function as buffers due to their ability to accept or donate protons, helping to resist changes in pH when acids or bases are added. This is due to the presence of both acidic and basic functional groups within the amino acid molecule.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979545,"front":"Explain the difference between the no charge form and the dipolar zwitterion form of an amino acid.","back":"The no charge form of an amino acid never occurs, while the dipolar zwitterion form is the most stable and exists in solution.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":35,"explanation":"The no charge form of an amino acid is theoretical and does not exist in reality due to the presence of both acidic and basic functional groups. On the other hand, the dipolar zwitterion form is the predominant and most stable form in solution due to internal ionization.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979546,"front":"What is the effect of pH on the form of amino acids with extra carboxylic acid or amine groups?","back":"In alkaline conditions, the extra carboxylic acid group will react and change form, while in acidic conditions, the extra amine group will react and change form.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":36,"explanation":"The pH level affects the ionization state of amino acids. In alkaline conditions, the carboxylic acid group becomes deprotonated, while in acidic conditions, the amine group becomes protonated. This influences the overall charge and form of the amino acid.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979547,"front":"What are dipeptides?","back":"Dipeptides are simple combination molecules of two amino acids with one amide (peptide) link.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":37,"explanation":"Dipeptides play a crucial role in protein synthesis and metabolism. They are formed through a dehydration reaction, where the carboxyl group of one amino acid bonds with the amino group of another, releasing water. This process is fundamental in creating larger peptides and proteins essential for various biological functions.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979548,"front":"How many possible combinations of amino acids are there in a dipeptide?","back":"For any two different amino acids, there are two possible combinations in a dipeptide.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":38,"explanation":"In a dipeptide, each position can be occupied by a different amino acid, resulting in two possible combinations. This is because the order matters, and each amino acid can only occupy one position in the dipeptide.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979549,"front":"Describe the reactions that can occur with the carboxylic acid and amine groups in amino acids.","back":"The carboxylic acid group and amine group in amino acids can undergo the usual reactions of these functional groups, such as esterification.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":39,"explanation":"Amino acids contain carboxylic acid and amine groups, which can undergo typical reactions of these functional groups. For instance, they can undergo esterification, among other reactions, due to the presence of these functional groups.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979550,"front":"What happens when proteins are heated with concentrated hydrochloric acid or strong alkalis?","back":"They can be hydrolysed and split back into their constituent amino acids.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":40,"explanation":"Heating proteins with concentrated hydrochloric acid or strong alkalis leads to hydrolysis, breaking peptide bonds. This process is crucial in digestion and protein analysis, allowing for the study of amino acid composition. It highlights the versatility of proteins and their susceptibility to environmental changes.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979551,"front":"How can the composition of a protein molecule be deduced?","back":"The composition of the protein molecule can be deduced by using TLC chromatography.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":41,"explanation":"TLC chromatography separates molecules based on their affinity for the stationary phase. Proteins will move at different rates depending on their composition, allowing for identification. This method is commonly used due to its simplicity and effectiveness in analyzing protein composition.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979552,"front":"Describe the process of splitting a protein into amino acids.","back":"A protein can be split into amino acids by reacting with concentrated hydrochloric acid.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":42,"explanation":"Proteins are made up of long chains of amino acids. When treated with concentrated hydrochloric acid, the peptide bonds holding the amino acids together are broken, resulting in the protein being split into its individual amino acid components.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979554,"front":"How can you ensure that the spots for each sample are equally spaced along the pencil line on the TLC plate?","back":"By drawing a pencil line 1 cm above the bottom of the TLC plate and marking spots for each sample equally spaced along the line.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":43,"explanation":"To achieve equal spacing, it's essential to use a ruler for precision. Marking spots at consistent intervals ensures uniformity, which is crucial for accurate comparison of sample migration. This method minimizes variability in results, leading to clearer separation and better analysis of the compounds.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979555,"front":"Define the Rf value in chromatography.","back":"The Rf value is calculated by dividing the distance moved by the amino acid by the distance moved by the solvent.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":44,"explanation":"The Rf value, or retention factor, is crucial in chromatography as it helps identify substances based on their movement relative to the solvent front. This ratio provides insight into the polarity and interaction of compounds with the stationary phase, aiding in the analysis and separation of complex mixtures.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979556,"front":"What is the purpose of spraying ninhydrin on the amino acids and heating them?","back":"Spraying ninhydrin on the amino acids and heating them causes red to blue spots to appear, making the transparent amino acids visible.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":45,"explanation":"Ninhydrin reacts with amino acids to form colored compounds, making them visible. Heating accelerates this reaction. This technique is used in chromatography to detect and visualize amino acids on a chromatogram.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979557,"front":"Describe the primary structure of proteins.","back":"The primary structure of proteins is the sequence of combinations of amino acids.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":46,"explanation":"The primary structure of proteins is crucial as it determines the overall protein function. It is a linear sequence of amino acids linked by peptide bonds. This sequence is encoded by the genetic information and dictates the protein's shape and function. Any alteration in this sequence can lead to changes in protein structure and function.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979558,"front":"What are proteins made from?","back":"Proteins are polymers made from combinations of amino acids.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":47,"explanation":"Proteins play crucial roles in biological processes, serving as enzymes, structural components, and signaling molecules. The sequence and composition of amino acids determine a protein's unique structure and function, highlighting the importance of genetic coding in protein synthesis.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979559,"front":"Define peptide links.","back":"Peptide links are the amide functional group that join amino acids together in proteins.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":48,"explanation":"Peptide links, also known as peptide bonds, are crucial in protein structure. They form through a condensation reaction between the carboxyl group of one amino acid and the amino group of another. This bond is central to the formation of polypeptide chains, which are the building blocks of proteins.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979560,"front":"How are amino acids linked together in proteins?","back":"Amino acids are linked together by condensation reactions with peptide links.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":49,"explanation":"Amino acids form proteins through peptide bonds, which are created during condensation reactions. This process involves the removal of a water molecule as the carboxyl group of one amino acid reacts with the amino group of another. The resulting chain of amino acids folds into specific structures, determining the protein's function.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979561,"front":"Describe the secondary structure of proteins.","back":"The secondary structure of proteins can take the form of an alpha-helix or a pleated sheet structure.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":50,"explanation":"Proteins' secondary structure is determined by hydrogen bonding patterns in the polypeptide chain. Alpha-helix has a coiled structure, while beta-pleated sheet has a more extended, sheet-like conformation. These structures are crucial for protein function and stability.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979562,"front":"What holds the alpha-helix structure of proteins in place?","back":"The alpha-helix structure of proteins is held in place by hydrogen bonds between the H of -N-H group and the -O of C=O of the fourth amino acid along the chain.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":51,"explanation":"The alpha-helix structure of proteins is stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another, forming a repeating pattern. This stabilizes the helical shape and contributes to the overall stability of the protein structure.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979563,"front":"How is the pleated sheet structure of proteins formed?","back":"The pleated sheet structure of proteins is formed when the protein chain folds into parallel strands held together by hydrogen bonds between the H of -N-H group and the -O of C=O of amino acids further along the chain in the parallel region.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":52,"explanation":"The pleated sheet structure, a key element of secondary protein structure, showcases the importance of hydrogen bonding in stabilizing protein conformation. This arrangement allows for efficient packing and contributes to the overall stability and functionality of proteins, influencing their biological roles and interactions.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979564,"front":"What is the role of R-groups in the secondary structure of proteins?","back":"The R-groups on the amino acids are all pointed to the outside of the alpha-helix structure of proteins.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":53,"explanation":"The orientation of R-groups on amino acids in the secondary structure of proteins is crucial for maintaining the stability and functionality of the structure. This arrangement allows for interactions with the surrounding environment, influencing the protein's properties and interactions with other molecules.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979565,"front":"What is the tertiary structure of proteins?","back":"The tertiary structure is the folding of the secondary structure into more complex shapes.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":54,"explanation":"The tertiary structure is crucial for a protein's functionality, as it determines how the protein interacts with other molecules. This folding is influenced by various interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions, which stabilize the overall shape and enable specific biological activities.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":979566,"front":"Describe the interactions that hold the tertiary structure in place.","back":"The tertiary structure is held in place by interactions between the R-side groups in more distant amino acids, including hydrogen bonding, sulfur-sulfur bonds, and ionic interactions.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":55,"explanation":"The tertiary structure of a protein is stabilized by various interactions between the R-groups of amino acids. These interactions include hydrogen bonding, disulfide bridges, and ionic interactions. These forces contribute to the overall folding and stability of the protein's 3D structure.","deleted_at":null,"flashcard_deck_id":"DfObg","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}}]

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