True or False: The following secondary structure shown below is an example of a beta-turn. True...
The secondary structure shown below is an example of an) N N A beta turn B. parallel beta sheet C antiparallel beta sheet D. right handed alpha helix Which amino acid would be most stabilizing at the N-terminus of an a-hellx (pH=7.0)? A Lysine B. Asparagine C Glutamine D. Glutamate
pls answer 6 and 7 6. Secondary structure (turn): The image below is of a polypeptide in secondary (20) structure level of protein folding. Specifically it is of a turn. Turns vary in length. The shorter the turn the more drastic the angle changes. The longer the turn, the more gradual the angles needed. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? Is this bond/interaction permanent or transient? d. What parts...
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino acid sequence defines the native structure of protein. b.) What is the main type of bonding responsible for stabilizing the secondary structure of proteins? c.) Briefly discuss the thermodynamics of protein folding into its native 3D structure. Is this process enthalpy driven or entropy driven? d.) Give an example of 2 major secondary structural motifs found in polypeptides. Do any of these motifs appear...
Match the super secondary structures/motifs shown below to their names a-a Greek key beta-a-beta P-hairpin In a two-step reaction (A a I a P), delta G^1 of the first step is 20 kJ/mol, and Delta G' of the second step is 80 kJ/mol. Which is the rate-limiting step, and why? Calculate the of a reaction needed to achieve a rate enhancement of 7.7 theta 10 degree at 37 degree C.
Distinguish between the different levels of protein structure, including primary, secondary, tertiary, and quaternary Question Is the following statement true? If not, explain why not: Since the secondary structure of a protein results from hydrogen bonding between components shared by all amino acids (a hydrogen on an amide N on one amino acid interacts with an oxygen on the carbonyl of another amino acid), the secondary structure does not depend on the specific amino acid groups (the R-groups) in the amino acid chain. Select...
Select True or False Shown here is the Lewis structure for the chloritelon CIO, that expands the octet to minimize formal charge and if necessary places negative formal charges on the most electronegative atomis) O True False
Beta (?β) sheets are a type of secondary structure in proteins. A segment of a single chain in an antiparallel ?β sheet has a length of 214 Å214 Å . How many residues are in this segment?
secondary hydrogens and _ tertiary 14. The structure shown below has hydrogens. We were unable to transcribe this image
Consider the following secondary structure map for answering the next two questions (where a means alpha helix and B means a beta strand) al B1 B2 a2 B3 Which two secondary structure elements would you be LEAST likely to find backbone hydrogen bonding interactions BETWEEN? O b1 and b2 a1 and 2 O b1 and b3 b2 and 13 Question 33 5 pts Which two secondary structure elements are MOST likely to be involved in forming parallel beta sheet interactions?...