Main-chain conformational tendencies of amino acids

被引:126
作者
Anderson, RJ
Weng, ZP
Campbell, RK
Jiang, XL
机构
[1] Serono Reprod Biol Inst, Rockland, MA 02370 USA
[2] Boston Univ, Dept Biomed Engn, Boston, MA USA
关键词
Ramachandran plot; folding tendency; two-dimensional map; diversity space; substitution table;
D O I
10.1002/prot.20530
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
A Rainachandran plot is a visual representation of the main-chain conformational tendencies of an amino acid. Despite forty years of research, the shape of Ramachandran plots is still a matter of debate. The issue in making a Ramachandran plot based on experimental data is deciding whether sparse data represent genuine conformations. We present here a simple solution to settle the ambiguities of the sparse data, and explain how we verified the accuracies of our plots using an independent dataset. To obtain our results, we then measured the pair-wise distances of main-chain conformational tendencies among amino acids, and showed that the conformational. relationships of amino acids are well preserved in a two-dimensional map, leading to the conclusion that the conformational. diversity space of amino acids is largely two dimensional. We further noticed that amino acids in early and late evolutionary stages are located in different zones in the two-dimensional map. In addition to these conclusions, we here present an amino acid substitution table derived from experimental data.
引用
收藏
页码:679 / 689
页数:11
相关论文
共 30 条
[1]  
[Anonymous], J MOL GRAPH
[2]   The ASTRAL compendium for protein structure and sequence analysis [J].
Brenner, SE ;
Koehl, P ;
Levitt, R .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :254-256
[3]   The interrelationships of side-chain and main-chain conformations in proteins [J].
Chakrabarti, P ;
Pal, D .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2001, 76 (1-2) :1-102
[4]   CONFORMATIONAL PARAMETERS FOR AMINO-ACIDS IN HELICAL, BETA-SHEET, AND RANDOM COIL REGIONS CALCULATED FROM PROTEINS [J].
CHOU, PY ;
FASMAN, GD .
BIOCHEMISTRY, 1974, 13 (02) :211-222
[5]   HIGH-RESOLUTION EPITOPE MAPPING OF HGH-RECEPTOR INTERACTIONS BY ALANINE-SCANNING MUTAGENESIS [J].
CUNNINGHAM, BC ;
WELLS, JA .
SCIENCE, 1989, 244 (4908) :1081-1085
[6]  
CUNNINGHAM BC, 1997, Patent No. 9711178
[7]  
FILIKOV A, 2000, Patent No. 0068385
[8]   An analysis of protein domain linkers: their classification and role in protein folding [J].
George, RA ;
Heringa, J .
PROTEIN ENGINEERING, 2002, 15 (11) :871-879
[9]   Disallowed Ramachandran conformations of amino acid residues in protein structures [J].
Gunasekaran, K ;
Ramakrishnan, C ;
Balaram, P .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 264 (01) :191-198
[10]   Revisiting the Ramachandran plot:: Hard-sphere repulsion, electrostatics, and H-bonding in the α-helix [J].
Ho, BK ;
Thomas, A ;
Brasseur, R .
PROTEIN SCIENCE, 2003, 12 (11) :2508-2522