What is the minimum number of residues to determine the secondary structural state?

被引:9
作者
Pan, XM [1 ]
Niu, WD [1 ]
Wang, ZX [1 ]
机构
[1] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源
JOURNAL OF PROTEIN CHEMISTRY | 1999年 / 18卷 / 05期
关键词
database size; local interactions; long-range interactions; secondary structure prediction;
D O I
10.1023/A:1020655417839
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The failure of protein secondary structural prediction is commonly attributed to the neglect of long-range interactions. The question is, what is the minimum length of subsequence required to determine the central secondary structural state, stabilized only by local interactions? In the present work, the 20 amino acids were classified into eight groups to analyze systematically the relationship between the length and secondary structural state of subsequences in the PDB database. It was found that the: fraction of subsequences with a unique central secondary structural state increases with increasing length, and the minimum length of subsequence required to determine the central secondary structural state is about 14-17 residues. The low accuracy of secondary structure prediction does not result from the neglect of long-range interactions, but may result from the limitation of the available protein database size or prediction algorithm.
引用
收藏
页码:579 / 584
页数:6
相关论文
共 15 条
[2]   PREDICTION OF PROTEIN CONFORMATION [J].
CHOU, PY ;
FASMAN, GD .
BIOCHEMISTRY, 1974, 13 (02) :222-245
[3]   ORIGINS OF STRUCTURAL DIVERSITY WITHIN SEQUENTIALLY IDENTICAL HEXAPEPTIDES [J].
COHEN, BI ;
PRESNELL, SR ;
COHEN, FE .
PROTEIN SCIENCE, 1993, 2 (12) :2134-2145
[4]   SECONDARY STRUCTURE ASSIGNMENT FOR ALPHA-BETA-PROTEINS BY A COMBINATORIAL APPROACH [J].
COHEN, FE ;
ABARBANEL, RM ;
KUNTZ, ID ;
FLETTERICK, RJ .
BIOCHEMISTRY, 1983, 22 (21) :4894-4904
[5]  
Fiser A, 1997, COMPUT APPL BIOSCI, V13, P297
[6]  
Garnier J, 1996, METHOD ENZYMOL, V266, P540
[7]   ON THE USE OF SEQUENCE HOMOLOGIES TO PREDICT PROTEIN-STRUCTURE - IDENTICAL PENTAPEPTIDES CAN HAVE COMPLETELY DIFFERENT CONFORMATIONS [J].
KABSCH, W ;
SANDER, C .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (04) :1075-1078
[8]   DICTIONARY OF PROTEIN SECONDARY STRUCTURE - PATTERN-RECOGNITION OF HYDROGEN-BONDED AND GEOMETRICAL FEATURES [J].
KABSCH, W ;
SANDER, C .
BIOPOLYMERS, 1983, 22 (12) :2577-2637
[9]   IMPROVEMENTS IN PROTEIN SECONDARY STRUCTURE PREDICTION BY AN ENHANCED NEURAL NETWORK [J].
KNELLER, DG ;
COHEN, FE ;
LANGRIDGE, R .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 214 (01) :171-182
[10]   TRIPLET INFORMATION IN HELIX PREDICTION APPLIED TO ANALYSIS OF SUPER-SECONDARY STRUCTURES [J].
NAGANO, K .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 109 (02) :251-274