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Questions and Answers
What structures are primarily stabilized by hydrogen bonds between carboxyl and amino groups?
What structures are primarily stabilized by hydrogen bonds between carboxyl and amino groups?
Which of the following amino acids is known to disrupt the formation of an α-helix?
Which of the following amino acids is known to disrupt the formation of an α-helix?
What is the number of amino acids present per turn in an α-helix?
What is the number of amino acids present per turn in an α-helix?
Which structural characteristic differentiates a β-sheet from an α-helix?
Which structural characteristic differentiates a β-sheet from an α-helix?
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What type of protein structure is primarily influenced by the arrangement of disulfide bonds?
What type of protein structure is primarily influenced by the arrangement of disulfide bonds?
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In which type of β-sheet are adjacent strands running in the same direction?
In which type of β-sheet are adjacent strands running in the same direction?
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Which statement correctly describes the stability of an α-helix?
Which statement correctly describes the stability of an α-helix?
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What defines the minor secondary structure known as β-bends?
What defines the minor secondary structure known as β-bends?
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Which of the following statements accurately describes oligomeric proteins?
Which of the following statements accurately describes oligomeric proteins?
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What is the primary structure of a protein primarily defined by?
What is the primary structure of a protein primarily defined by?
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Which of the following is an example of a protein that exhibits secondary structure?
Which of the following is an example of a protein that exhibits secondary structure?
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What characterizes the tertiary structure of proteins?
What characterizes the tertiary structure of proteins?
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What is a significant consequence of a change in the primary structure of a protein?
What is a significant consequence of a change in the primary structure of a protein?
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Which of the following is true about the quaternary structure of proteins?
Which of the following is true about the quaternary structure of proteins?
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What distinguishes a monomeric protein from an oligomeric protein?
What distinguishes a monomeric protein from an oligomeric protein?
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Which of the following examples correctly represents the quaternary structure?
Which of the following examples correctly represents the quaternary structure?
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What is the primary characteristic of β-bends in protein structure?
What is the primary characteristic of β-bends in protein structure?
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Which of the following statements is true regarding tertiary structure of proteins?
Which of the following statements is true regarding tertiary structure of proteins?
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What happens to a protein during denaturation?
What happens to a protein during denaturation?
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Which type of bond is primarily responsible for stabilizing quaternary protein structures?
Which type of bond is primarily responsible for stabilizing quaternary protein structures?
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What effect does denaturation have on the solubility of proteins?
What effect does denaturation have on the solubility of proteins?
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Which of the following agents is NOT a physical denaturing agent?
Which of the following agents is NOT a physical denaturing agent?
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Which feature distinguishes oligomeric proteins from monomeric proteins?
Which feature distinguishes oligomeric proteins from monomeric proteins?
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Which amino acids are most likely involved in forming kinks in the polypeptide chain?
Which amino acids are most likely involved in forming kinks in the polypeptide chain?
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What is the process called when the carboxyl group of one amino acid links with the amino group of another amino acid to form a peptide?
What is the process called when the carboxyl group of one amino acid links with the amino group of another amino acid to form a peptide?
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What suffix do amino acid residues have when peptides are named, excluding the free C-terminal amino acid?
What suffix do amino acid residues have when peptides are named, excluding the free C-terminal amino acid?
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Which of the following is NOT a function of glutathione?
Which of the following is NOT a function of glutathione?
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What is the primary role of oxytocin in the body?
What is the primary role of oxytocin in the body?
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Angiotensin II is derived from which peptide and has what primary effect?
Angiotensin II is derived from which peptide and has what primary effect?
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Which peptide is known for its opiate-like function and helps inhibit pain?
Which peptide is known for its opiate-like function and helps inhibit pain?
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Which type of peptides are produced from plasma proteins through snake venom enzymes?
Which type of peptides are produced from plasma proteins through snake venom enzymes?
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What is the primary effect of denaturation on the protein structure?
What is the primary effect of denaturation on the protein structure?
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What is the primary component that makes up aspartame?
What is the primary component that makes up aspartame?
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Which type of protein is characterized as being water-soluble and spherical in shape?
Which type of protein is characterized as being water-soluble and spherical in shape?
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Which bonding force plays a crucial role in stabilizing the tertiary structure of proteins?
Which bonding force plays a crucial role in stabilizing the tertiary structure of proteins?
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What characteristic is NOT associated with fibrous proteins?
What characteristic is NOT associated with fibrous proteins?
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Which of the following agents is classified as a chemical denaturing agent?
Which of the following agents is classified as a chemical denaturing agent?
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What occurs during protein folding?
What occurs during protein folding?
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Which type of globular protein is soluble in dilute salt solutions and heat-coagulated?
Which type of globular protein is soluble in dilute salt solutions and heat-coagulated?
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In the context of β-bends, what term is used to describe the resulting structure due to specific hydrogen bonds?
In the context of β-bends, what term is used to describe the resulting structure due to specific hydrogen bonds?
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Which of the following proteins is considered a conjugated protein due to the presence of a nucleic acid?
Which of the following proteins is considered a conjugated protein due to the presence of a nucleic acid?
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What is a key feature of lectins in biological systems?
What is a key feature of lectins in biological systems?
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Which of the following is a type of fibrous protein found in exoskeletal structures?
Which of the following is a type of fibrous protein found in exoskeletal structures?
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Which gastrointestinal hormone is involved in digestive processes?
Which gastrointestinal hormone is involved in digestive processes?
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Which of the following amino acid types is typically found in high amounts in keratin?
Which of the following amino acid types is typically found in high amounts in keratin?
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What is the property of proteins that is used in ion exchange chromatography?
What is the property of proteins that is used in ion exchange chromatography?
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Which technique relies on a protein's molecular size for separation?
Which technique relies on a protein's molecular size for separation?
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What does isoelectric focusing depend on for the cessation of protein movement?
What does isoelectric focusing depend on for the cessation of protein movement?
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Which property does the technique 'salting out' utilize for protein purification?
Which property does the technique 'salting out' utilize for protein purification?
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In two-dimensional electrophoresis, what properties of proteins are used for their separation?
In two-dimensional electrophoresis, what properties of proteins are used for their separation?
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What is the significance of dialysis in protein purification?
What is the significance of dialysis in protein purification?
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Which property is exploited in adsorption chromatography?
Which property is exploited in adsorption chromatography?
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What fundamental property does polyacrylamide gel electrophoresis (PAGE) utilize?
What fundamental property does polyacrylamide gel electrophoresis (PAGE) utilize?
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What is the main factor determining the efficiency of ultracentrifugation?
What is the main factor determining the efficiency of ultracentrifugation?
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Which method would be ineffective in separating proteins based on their molecular size?
Which method would be ineffective in separating proteins based on their molecular size?
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What is the primary determinant of a protein's biological activity?
What is the primary determinant of a protein's biological activity?
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Which of the following proteins represents an example of an oligomeric protein?
Which of the following proteins represents an example of an oligomeric protein?
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What distinguishes the tertiary structure of a protein from its secondary structure?
What distinguishes the tertiary structure of a protein from its secondary structure?
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Which characteristic accurately describes the quaternary structure of proteins?
Which characteristic accurately describes the quaternary structure of proteins?
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What is the significance of a change in the primary structure of a protein?
What is the significance of a change in the primary structure of a protein?
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Which level of protein structure is primarily determined by interactions between amino acids that are close in sequence?
Which level of protein structure is primarily determined by interactions between amino acids that are close in sequence?
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How many amino acids comprise the A chain of insulin?
How many amino acids comprise the A chain of insulin?
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Which of the following statements is true about monomeric proteins?
Which of the following statements is true about monomeric proteins?
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Which type of protein structure is stable due to covalent peptide bonds?
Which type of protein structure is stable due to covalent peptide bonds?
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Which protein exemplifies a quaternary structure with four globin chains?
Which protein exemplifies a quaternary structure with four globin chains?
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Study Notes
Protein Chemistry
- Proteins are the most abundant organic molecules in living systems
- They make up approximately 50% of cellular dry weight
- Proteins are fundamental to structure and function of life
- Protein chemistry studies the structure, function, and properties of proteins
- Proteins are polymers of amino acids linked by peptide bonds
- The peptide bond is a covalent bond between the carboxyl group of one amino acid and the amino group of another
- Peptide bonds are anhydride bonds formed by the loss of water molecule
- Two amino acids form a dipeptide, three a tripeptide, four a tetrapeptide, etc
- Ten to fifty amino acids form an oligopeptide. Chains with more than 50 are called proteins
- The N-terminal end has a free alpha amino group, named after the first amino acid
- The C-terminal end has a free alpha carboxyl group, contributed by the last amino acid
- Peptide nomenclature involves appending a -yl suffix to all amino acid residues except the C-terminal one.
- Examples of physiologically important peptides:
- Glutathione (a tripeptide composed of gamma-glutamyl-cysteinyl-glycine) with functions in RBC membrane integrity, protecting hemoglobin, and amino acid transport
- Thyrotropin releasing hormone (TRH)
- Oxytocin
- Vasopressin
- Angiotensins
- Methionine enkephalin
- Bradykinin and kallidin
- Peptide antibiotics (e.g., gramicidin, bacitracin, tyrocidin)
- Aspartame
- Gastrointestinal hormones (e.g., gastrin, secretin)
Protein Classification
-
Simple proteins: Composed only of amino acids.
- Globular proteins (e.g., albumins, globulins, glutelins, prolamines, histones, globins, protamines, lectins, ) are generally soluble; some notable examples include serum albumin, ovalbumin, and casein in milk.
- Scleroproteins (e.g., collagens, elastins, keratins) are insoluble and crucial for structural support.
-
Conjugated proteins: Contain a non-protein moiety (prosthetic group).
- Nucleoproteins (e.g., nucleohistones, nucleoprotamines)
- Glycoproteins
- Lipoproteins
- Phosphoproteins
- Chromoproteins
- Metalloproteins.
- Derived proteins: Denatured or degraded products of simple and conjugated proteins.
Protein Classification based on function:
- Structural: Keratin, collagen
- Enzymes: Hexokinase, pepsin
- Transport : Hemoglobin, serum albumin
- Hormonal: Insulin, growth hormone
- Contractile : Actin, myosin
- Storage : Ovalbumin, glutelin
- Genetic : Nucleoproteins
- Defence: Snake venoms, Immunoglobulins
- Receptor: For hormones, viruses
Protein Purification Techniques
- Purifying protein from extraction buffer (e.g., ion exchange chromatography, gel filtration chromatography, affinity chromatography, adsorption chromatography)
- Electrophoretic techniques (e.g., Polyacrylamide Gel Electrophoresis (PAGE), Isoelectric focusing,2-Dimensional electrophoresis, Gradient Gel Electrophoresis)
- Other techniques (e.g. ultracentrifugation, salting out, dialysis)
Protein Folding
- Proteins fold into their biologically active 3D shapes through a complex process
- Folding influenced by various external factors including pH, temperature, chemicals, and limitations in space
- Protein misfolding can lead to problems and diseases.
- Protein misfolding may cause amyloid disorders (e.g. Alzheimer's disease).
- Prion diseases are another example of protein misfolding (e.g., Creutzfeldt-Jakob disease, Kuru, scrapie, BSE)
Protein Denaturation
- Denaturation is the process where a protein loses its native structure without breaking primary structure
- Chemical denaturation agents include acids, alkalis, organic solvents, heavy metals, urea, and others.
- Physical denaturation agents include heat, UV radiation, X-rays, ultrasound, and pressure.
- Denaturation affects solubility, precipitability, and biological activity of proteins, making them more digestible.
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Description
This quiz covers the fundamentals of protein chemistry, including their structure, function, and properties. Explore concepts such as peptide bonds, amino acids, and nomenclature. Understand the significance of proteins in living systems and their classification based on amino acid chains.