This means that the amino-acid sequence contains all of the information that is required for the polypeptide chain to fold up into a discrete three-dimensional shape The three-dimensional structure is determined by the amino-acid sequence. The primary sequence of RNase is sufficient to determine its specific secondary and tertiary structureĪny given protein is characterized by a unique amino acid sequence (primary structure) and three-dimensional (tertiary) structure. They may retain their correct shape even when separated from the rest of the protein.Įxperiments on denaturation and renaturation after the reduction and reoxidation of the -S-S- bonds in the enzyme ribonuclease (RNase) have shown that: Which of the following statements concerning protein domains is true? Proteins often have regions that can fold and function as an independent entity from the whole protein. The sequence is most probably part of a(n): Have weaker hydrogen bonds laterally between adjacent strandsĪmino acid residues commonly found in the middle of beta turn are:Ī sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly. The major reason that antiparallel beta-stranded protein structures are more stable than parallel beta-stranded structures is that the latter: The presence of two Lys residues near the amino terminus of the alpha helix. Steric hindrance occurs between the bulky Thr side chainsĪn alpha helix would be destabilized most by: Thr and/or Leu residues tend to disrupt an alpha helix when they occur next to each other in a protein because: In an alpha helix, the R groups on the amino acid residues:Īre found on the outside of the helix spiral Roughly how many amino acids are there in one turn of an alpha helix?Īre roughly parallel to the axis of the helix Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds? Peptide bonds are essentially planar, with no rotation about the C-N axis Pauling and Corey’s studies of the peptide bond showed that: They can interact with multiple protein-binding partners and are central to protein interaction networks. Which statement about intrinsically disordered proteins is true? Which of the following is not an appropriate description for van der Waals interactions? Placement of hydrophobic amino acid residues within the interior of the protein. One is the formation of the maximum number of hydrogen bonds. In an aqueous solution, protein conformation is determined by two major factors. The most important contribution to the stability of a protein’s conformation appears to be the:Įntropy increase from the decrease in ordered water molecules forming a solvent shell around it. All of the following are considered “weak” interactions in proteins except:
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