Anisotropic network model: systematic evaluation and a new web interface

被引:263
作者
Eyal, Eran [1 ]
Yang, Lee-Wei [1 ]
Bahar, Ivet [1 ]
机构
[1] Univ Pittsburgh, Dept Computat Biol, Sch Med, Pittsburgh, PA 15213 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1093/bioinformatics/btl448
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Motivation: The Anisotropic Network Model (ANM) is a simple yet powerful model for normal mode analysis of proteins. Despite its broad use for exploring biomolecular collective motions, ANM has not been systematically evaluated to date. A lack of a convenient interface has been an additional obstacle for easy usage. Results: ANM has been evaluated on a large set of proteins to establish the optimal model parameters that achieve the highest correlation with experimental data and its limits of accuracy and applicability. Residue fluctuations in globular proteins are shown to be more accurately predicted than those in nonglobular proteins, and core residues are more accurately described than solvent-exposed ones. Significant improvement in agreement with experiments is observed with increase in the resolution of the examined structure. A new server for ANM calculations is presented, which offers flexible options for controlling model parameters and output formats, interactive animation of collective modes and advanced graphical features.
引用
收藏
页码:2619 / 2627
页数:9
相关论文
共 55 条
[21]   WEBnm@: a web application for normal mode analyses of proteins [J].
Hollup, SM ;
Salensminde, G ;
Reuter, N .
BMC BIOINFORMATICS, 2005, 6 (1)
[22]   VMD: Visual molecular dynamics [J].
Humphrey, W ;
Dalke, A ;
Schulten, K .
JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1996, 14 (01) :33-38
[23]   Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: Structure and collective motions [J].
Hung, A ;
Tai, K ;
Sansom, MSP .
BIOPHYSICAL JOURNAL, 2005, 88 (05) :3321-3333
[24]   Functional motions of influenza virus hemagglutinin: A structure-based analytical approach [J].
Isin, B ;
Doruker, P ;
Bahar, I .
BIOPHYSICAL JOURNAL, 2002, 82 (02) :569-581
[25]   DICTIONARY OF PROTEIN SECONDARY STRUCTURE - PATTERN-RECOGNITION OF HYDROGEN-BONDED AND GEOMETRICAL FEATURES [J].
KABSCH, W ;
SANDER, C .
BIOPOLYMERS, 1983, 22 (12) :2577-2637
[26]   Relating molecular flexibility to function: A case study of tubulin [J].
Keskin, O ;
Durell, SR ;
Bahar, I ;
Jernigan, RL ;
Covell, DG .
BIOPHYSICAL JOURNAL, 2002, 83 (02) :663-680
[27]  
KONDRASHOV DA, 2006, BIOPHYS J, DOI DOI 10.1529/BIOPHYSJ.106.85894
[28]   Normal mode analysis of macromolecular motions in a database framework: Developing mode concentration as a useful classifying statistic [J].
Krebs, WG ;
Alexandrov, V ;
Wilson, CA ;
Echols, N ;
Yu, HY ;
Gerstein, M .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2002, 48 (04) :682-695
[29]   Dynamics of proteins in crystals: Comparison of experiment with simple models [J].
Kundu, S ;
Melton, JS ;
Sorensen, DC ;
Phillips, GN .
BIOPHYSICAL JOURNAL, 2002, 83 (02) :723-732
[30]   A coarse-grained normal mode approach for macromolecules:: An efficient implementation and application to Ca2+-ATPase [J].
Li, GH ;
Cui, Q .
BIOPHYSICAL JOURNAL, 2002, 83 (05) :2457-2474