Which of the following is not known to be involved in the process of assisted folding of proteins? OA) Chaperonins OB) Disulfide interchange OC) Heat shock proteins OD) Peptide bond hydrolysis OE) Peptide bond isomerization
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- 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-EProtein synthesis in bacterial cells usually starts with a: phenylalanine residue. alanine residue. methionine residue. formylmethionine residue.What drives spontaneous folding into the correct tertiary structure for a newly synthesized protein?
- Once modified, do proteins always have the correct threedimensional structure?Which of the following peptides will likely adopt an alpha helix structure? (idk) A-D-I-E-L-Y-F-H-I-C-V-D A-R-E-P-H-Y-D-P-C-Q-S A-D-I-E-L-Y-M-H-I-C-V-D A-R-E-V-H-Y-I-D-C-Q-FWhich of the following peptides will likely adopt an alpha helix? H-I-R-E-F A-D-L-E-E A-D-E-L-E C-V-D-E-F
- Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary)as defined for proteins.(a) What level is shown by double-stranded DNA?(b) What level is shown by tRNA?(c) What level is shown by mRNA?A protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helices