Folding simulations of alanine-based peptides with lysine residues.

Abstract:

:The folding of short alanine-based peptides with different numbers of lysine residues is simulated at constant temperature (274 K) using the rigid-element Monte Carlo method. The solvent-referenced potential has prevented the multiple-minima problem in helix folding. From various initial structures, the peptides with three lysine residues fold into helix-dominated conformations with the calculated average helicity in the range of 60-80%. The peptide with six lysine residues shows only 8-14% helicity. These results agree well with experimental observations. The intramolecular electrostatic interaction of the charged lysine side chains and their electrostatic hydration destabilize the helical conformations of the peptide with six lysine residues, whereas these effects on the peptides with three lysine residues are small. The simulations provide insight into the helix-folding mechanism, including the beta-bend intermediate in helix initiation, the (i, i + 3) hydrogen bonds, the asymmetrical helix propagation, and the asymmetrical helicities in the N- and C-terminal regions. These findings are consistent with previous studies.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Sung SS

doi

10.1016/S0006-3495(95)80259-6

subject

Has Abstract

pub_date

1995-03-01 00:00:00

pages

826-34

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(95)80259-6

journal_volume

68

pub_type

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