Molecular dynamics simulations of a winter flounder "antifreeze" polypeptide in aqueous solution.

Abstract:

:A winter flounder antifreeze polypeptide (HPLC-6) has been studied in vacuo and in aqueous solution using molecular dynamics computer simulation techniques. The helical conformation of this polypeptide was found to be stable both in vacuum and in solution. The major stabilizing interactions were found to be the main-chain hydrogen bonds, a salt-bridge interaction, and solute-solvent hydrogen bonds. A significant bending in the middle of the polypeptide chain was observed both in vacuo and in solvent at 300 K. Possible causes of the bending are discussed. From simulations of mutant polypeptide molecules in vacuo, it is concluded that the bend in the native polypeptide was caused by side chain to backbone hydrogen bond competition involving the Thr 24 side chain and facilitated by strains on the helix resulting from the Lys 18-Glu 22 salt bridge.

journal_name

Biopolymers

journal_title

Biopolymers

authors

McDonald SM,Brady JW,Clancy P

doi

10.1002/bip.360331002

subject

Has Abstract

pub_date

1993-10-01 00:00:00

pages

1481-503

issue

10

eissn

0006-3525

issn

1097-0282

journal_volume

33

pub_type

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