In extracellular proteins the amino acid Cys can interact with another Cys to form a bond sometimes called _______. The formation of this covalent bond is reaction. a. O b. disulfide, cystine, oxidizing O c. disulfide, cysteine, reducing d. disulfide, cystine, dehydration e. peptide, polypeptide, oxidizing peptide, polypeptide, condensation
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- Proteins can be precipitated out of aqueous solution bythe addition of an electrolyte; this process is called “saltingout” the protein. (a) Do you think that all proteins wouldbe precipitated out to the same extent by the same concentrationof the same electrolyte? (b) If a protein has beensalted out, are the protein–protein interactions stronger orweaker than they were before the electrolyte was added?Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactionsAlthough all of these may play a part, the major driving force in protein folding is: a) hydrogen bond formation b) salt bridge formation c) steric interactions d) the hydrophobic effect A partially folded protein is called a a) peptide template b) active domain c) molten globule d) precursor protein Which of these processed is NOT seen in protein denaturation? A) subunits are dissociated b) folding is unraveled c) alpha helix and beta sheets are unraveled d) peptide bonds are broken. A protein which has more than one stable conformation is called a: a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein If a denatured protein does not spontaneously renature upon removal of denaturing agents, it may require a ____ to renature. a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein Prion protein and amyloid protein have which trait in common? A) They denature very easily…
- Tertiary structure of protein is maintained by Select one: a. Hydrogen bond b. All of these c. Di-sulphide bond d. Peptide bondWhich of these statements about hemoglobin is NOT true? A) it is a tetrameric globular protein b) it has a prosthetic group called heme c) it’s dominant motif is beta barrel d) its dominant motif is helix-turn-helix The reagent used to break disulfide bonds is: a) urea b) beta-mercaptoethanol c) guanidine hydrochloride d) phosphorus pentachlorideAt what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)
- Protein β-sheets are most likely to be found in: a either the interior or exterior of proteins, with no preference for one or the other. b the exterior of proteins, exposed to the aqueous environment. c the interior of proteins, away from the aqueous environment.Which of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptideWhich of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
- When an amino acid's side chain, such as aspartic acid, has a pKa, that pKa is not the same if the amino acid occurs on the interior of a protein. Why would the pKa of a side chain of an Asp occuring on the inside of a protein be different from an Asp on the outside of a protein?Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsIndicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond