Intrinsically disordered proteins may:
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Question 39 options:
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lack a hydrophobic core.
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All of the answers are correct.
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wrap around their targets.
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have multiple interaction partners.
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Solved in 3 steps
- Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryDenaturation of protein is a loss of protein structure. Given enough time, can all denatured protein spontaneously renature? Justify answerWhich of the following levels of protein structure can involve covalent bond formation? A) Primary B) Secondary C) Teritary D) Quaternary E) Primary and teritary F) Primary, teritary and quaternary
- Describe the different orders of protein structure, the different functions of proteins, and how protein structure grants specificity of function.Which of the following amino acids would be most soluble in water? Group of answer choices glycine at pH 8 proline at pH 6 valine at pH 1 leucine at pH 4 alanine at pH 7Protein denaturation usually refers to the disruption of which of the following types of molecular interactions? Select all that apply. A.)Van der Waals attraction B.)Covalent bonds C.)Hydrogen bonds D.)Hydrophobic interactions
- At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acidsWhich of the following is the distinguishing factor of a protein? The backbone of the protein chain Its solubility The side chains of the protein chain The prosthetic groupName and discuss the non covalent interactions that maintain protein structure
- Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the aboveWhen a small, globular protein unfolds, which of the following are true? (SELECT ALL THAT APPLY) Choice 1 of 6: the temperature must increase Choice 2 of 6: the entropy of the peptide backbone increases Choice 3 of 6: the entropy of the solvent waters increases Choice 4 of 6: H bonds between peptide backbone atoms must break Choice 5 of 6: new attractive interactions form between water and side chains Choice 6 of 6: a detergent molecule must be added
