Look-up tables for protein solvent accessibility prediction and nearest neighbor effect analysis.

Abstract:

:We developed dictionaries of two-, three-, and five-residue patterns in proteins and computed the average solvent accessibility of the central residues in their native proteins. These dictionaries serve as a look-up table for making subsequent predictions of solvent accessibility of amino acid residues. We find that predictions made in this way are very close to those made using more sophisticated methods of solvent accessibility prediction. We also analyzed the effect of immediate neighbors on the solvent accessibility of residues. This helps us in understanding how the same residue type may have different accessible surface areas in different proteins and in different positions of the same protein. We observe that certain residues have a tendency to increase or decrease the solvent accessibility of their neighboring residues in C- or N-terminal positions. Interestingly, the C-terminal and N-terminal neighbor residues are found to have asymmetric roles in modifying solvent accessibility of residues. As expected, similar neighbors enhance the hydrophobic or hydrophilic character of residues. Detailed look-up tables are provided on the web at www.netasa.org/look-up/.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Wang JY,Ahmad S,Gromiha MM,Sarai A

doi

10.1002/bip.20113

subject

Has Abstract

pub_date

2004-10-15 00:00:00

pages

209-16

issue

3

eissn

0006-3525

issn

1097-0282

journal_volume

75

pub_type

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