WDANIKQRLSTEYKQ (a) How many full turns are in this a-helix? (b) What is the length of the helix (in Angströms) in the direction of the helix axis? (c) How many hydrogen bonds between the backbone atoms are in this helix? Explain your reasoning. (d) In the protein, one side of this helix is facing the hydrophobic core of the protein, and the other side is facing the aqueous solvent. Circle the residues involved in the hydrophobic contacts. Underline those residues that favor contacts with water. (e) What would you predict the effect of each of the following mutations to be on the stability of the helix? Explain your reasoning. 1. I->A 2. R->A 3. E->R 4. W->P
Neutral Amino Acids
Amino acids which do not have any charge on them are neutral amino acids.
Globular Protein
The globular proteins refer to the shape of protein specifically spherical in nature apart from spherical form fibrous, disordered and membrane-bound proteins exist. These globular proteins are miscible in water and form a colloidal solution rather than other types which might not exhibit solubility. Many classes of the fold are found in globular proteins, which render them a sphere shape. Globular fold containing proteins usually are referred to by the term globin.
Dimer
Dimers are basic organic compounds, which are derivates of oligomers. It is formed by the combination of two monomers which could potentially be strong or weak and in most cases covalent or intermolecular in nature. Identical monomers are called homodimer, the non-identical dimers are called heterodimer. The method by which dimers are formed is known as “dimerization”.
Dipeptide
A dipeptide is considered a mixture of two distinct amino acids. Since the amino acids are distinct, based on their composition, two dipeptide's isomers can be produced. Various dipeptides are biologically essential and are therefore crucial to industry.
4. *** Consider an a-helix with the following sequence:
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