Some regions of protein secondary structure are described as "random coil". This designation is misleading because:
A. the secondary structure must always be an alpha helix or beta sheet.
B. although the structure is indeed random, it need not necessarily resemble a "coil".
C. although the region may be unique to a particular protein, it is not random: each cellular copy of that protein will contain an identical "random coil" structure that corresponds to the same portion of primary sequence.
D. an alpha helix represents one type of "coil", but its structure is certainly not random.
E. actually all types of secondary structure are random in nature.
Answer:
The answer for the above statement is (A) i.e., the secondary structure must always be an alpha helix or beta sheet.
Explanation:
Random coil : A protein that completely lacks secondary structure is random coil.
In random coil, the only fixed relationships between amino acids is that between adjacent residues through the peptide bond.
as a result random coils can be detected from the absence of signals in multi dimensional nuclear magnetic resonance experiment that depend on particular peptide-peptide interaction. Random coil is easily distinguished by circular dichroism.
Denaturing reduces a protein entirely to a random coil.
Some regions of protein secondary structure are described as "random coil". This designation is misleading because:...
The synthetic polyethene, -(CHXCH_2) -, has a random coil structure. Here, (CHXCH_2) refers to its ____ structure, and random coil is its ____structure. (a) primary (b) secondary or tertiary (c) tertiary or quaternary (d) quaternary. The proteins can have the alpha-helix and beta-sheet structures. The alpha-helix refers to the ____ structures and the beta-sheet refers to the ___ structure. (a) primary (b) secondary or tertiary (c) tertiary or quaternary (d) quaternary. The types of base parings in double helical DNA...
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....
1. What is NOT TRUE regarding a phospholipid bilayer? A. The two leaflets of the bilayer are identical. B. It takes energy to flip one phospholipid from one side to the other C. In animal cells cholesterol is inserted into the bilayer D. The bilayer can contain more than one type of phospholipid. 2. New membrane is made and assembled in the ___ and delivered to the plasma membrane in vesicles derived from the _. A. Cytosol; ER B. Cytosol;...
a. Using the table below, predict the secondary structure most
likely adopted by the heptapeptide "RANGEHEAL". Will it be
alpha-helical, beta-strand, or just random coil?
b. Hydrogen bonds between backbone residues stabilize
interactions between
helixes and
sheets. Knowing this and other information about hydrogen bonds,
which amino acid from the picture below will destabilize secondary
protein structure?
Conformational Preferences of the Amino Acids Preference Amino acid a-helix B-strand Reverse turn Glu 1.59 0.52 1.01 Ala 1.41 0.72 0.82...