OPTIMAL PROTEIN-FOLDING CODES FROM SPIN-GLASS THEORY

被引：334

作者：

GOLDSTEIN, RA

LUTHEYSCHULTEN, ZA

WOLYNES, PG

机构：

[1] UNIV ILLINOIS, NATL CTR SUPERCOMP APPLICAT, URBANA, IL 61801 USA

[2] UNIV ILLINOIS, BECKMAN INST, URBANA, IL 61801 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 11期

关键词：

PROTEIN-STRUCTURE PREDICTION; ASSOCIATIVE MEMORIES; NEURAL NETWORKS; BIOMOLECULAR DYNAMICS;

D O I：

10.1073/pnas.89.11.4918

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Protein-folding codes embodied in sequence-dependent energy functions can be optimized using spin-glass theory. Optimal folding codes for associative-memory Hamiltonians based on aligned sequences are deduced. A screening method based on these codes correctly recognizes protein structures in the "twilight zone" of sequence identity in the overwhelming majority of cases. Simulated annealing for the optimally encoded Hamiltonian generally leads to qualitatively correct structures.

引用

页码：4918 / 4922

页数：5

共 22 条

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