1. What secondary structure elements comprise each zinc finger? 2. What holds together the fold of an individual zinc finger domain
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1. What secondary structure elements comprise each zinc finger?
2. What holds together the fold of an individual zinc finger domain?
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- (a) In what important ways do the α helix and β sheet structures differ? (b) How are they similar?1. 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…Which dastardly proteins help polypeptides fold into an incorrect and non-functional state?
- 1. 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.13. What are the two noncontractile proteins? 14. What is the function of the two noncontractile proteins?Which proteins help other polypeptides to fold into the right shape?
- What are the 4 levels of structural organization of proteins and what are the important interactions that stabilize these structural levels?Why do alpha and beta tubulin monomers differ in sequence by 60%?For the three peptides below, label whether they would form an amphiphilic beta-strand, amphiphilic helix, or nothing. Explain why. Part a) S-V-K-I-Q-M-R-A-D-L Part b) A-L-E-H-M-F-R-Y-L-A-K Part c) A-L-A-I-W-F-P-D-R-K-E
- 17.5.) If a mutation in an organism's DNA causes the resulting protein to possess a glutamine instead of a glycine in the 13th position, what level(s) of the resulting protein's structure would potentially be affected? Why?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 amino acids from beginning to end of molecule