Side-chain interactions in the C-peptide helix: Phe 8 ... His 12+.

Abstract:

:Previous studies have demonstrated that His 12 plays a major role in the pH-dependent stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A). Here, amino acid replacement experiments show that His 12+ stabilizes the C-peptide helix chiefly by interacting with Phe 8. The Phe 8 ... His 12+ ring interaction is specific for the protonated form of His 12 (His 12+) and the interaction is not screened significantly by NaCl, unlike the charged group ... helix dipole interactions studied earlier in C-peptide. Analogs of C-peptide that are unable to form the Phe 8 ... His 12+ interaction show large increases in helix content for Phe----Ala and His----Ala. Therefore, the helical tendencies of the individual residues Phe, His, and Ala are important in determining the result of a replacement experiment. Since the side chains of Phe 8 and His 12 probably interact within the N-terminal helix of ribonuclease A, the existence of the Phe 8 ... His 12+ interaction in the isolated C-peptide helix adds to the evidence that the C-peptide helix is an autonomous folding unit.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Shoemaker KR,Fairman R,Schultz DA,Robertson AD,York EJ,Stewart JM,Baldwin RL

doi

10.1002/bip.360290104

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

1-11

issue

1

eissn

0006-3525

issn

1097-0282

journal_volume

29

pub_type

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