What type of interactions is primarily responsible for the creation of the following type of structures? a) Covalent Bonding b) Ionic Interactions c)H-bonding d) Hydrophobic interactions 1. a in the formation of a protein's primary structure in the formation of an alpha helix in the formation of a protein's tertiary structure 2. C 3. d
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- a. Can a mutation change a proteins tertiary structure without changing its primary structure? b. Can a mutation change a proteins primary structure without affecting its secondary structure?Which of the following is primarily responsible for stabilizing the a-helix, a type of 1. secondary structure formed by a single nolvpeptide chain? hydrophobic interactions hydrogen bonds of backbone ionic interactions disulfide bridges hydrogen bonds involving the R-side chains a) b) atoms d) The atoms that make up the peptide bond that links amino acids together in a protein are in the same plane (coplanar). In the a-helix, how are these peptide bond planes arranged? 2. a) perpendicular to the a-helix approximately parallel to a-helix axis b) both parallel and perpendicular to the a-helix randomly oriented with respect to the axis of the a-helix peptide bond planes don't exist in the a-helix1. Which best describes the contribution of primary (1’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule. 2. What shapes result from secondary structure: a) β- helix & α-sheets b) α-helix and β-sheets c) ɗ-bilayers & β-domains d) µ-folds 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of…
- The structure shown below belongs to which family of protein tertiary structure? PDB: 1Z4A 1) a/ß barrel 2) B-barrel 3) a-helix bundle 4) aß-sandwichThe structure shown below belongs to which family of protein tertiary structure? 1) x/B barrel 2) B-barrel 3) x-helix bundle 4) xß-sandwich PDB: 1VRD1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?
- Which of the following features correctly describe aspects of protein structure? a) A protein possessing disulfide bonds will be more stable than a protein with the identical primary sequence lacking disulfide bonds. O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands. c) Folding of a protein (tertiary structure) will typically result in a majority of the non-polar amino acids being distributed on the protein surface. d) both a and cIn most cases the peptide bond is in the trans conformation. What statement below best explains this observation? a) The peptide bond has double bond character that prevents free rotation. b) In the cis conformation the R groups cause steric hindrance. c) In the trans conformation the carbonyl oxygen and the amine hydrogen can participate in hydrogen bonding. d) In the trans conformation the angle strain is reduced. e) All of the above explain the observation. while all statements might be true they do not explain the phenomenonWhich of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
- Protein 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 interactionsProper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structureWhich one of the following types of bond is principally responsible for holding the α-helix shape of a protein secondary structure : A) peptide B) disulfide C) hydrogen D)ionic