ASAView: Database and tool for solvent accessibility representation in proteins

被引:227
作者
Ahmad, S [1 ]
Gromiha, M
Fawareh, H
Sarai, A
机构
[1] Kyushu Inst Technol, Dept Biochem Engn & Sci, Iizuka, Fukuoka 8208502, Japan
[2] Natl Inst Adv Ind Sci & Technol, CBRC, Koto Ku, Tokyo, Japan
[3] Zarka Private Univ, Dept Comp Sci, Zarka 13110, Jordan
关键词
D O I
10.1186/1471-2105-5-51
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Background: Accessible surface area (ASA) or solvent accessibility of amino acids in a protein has important implications. Knowledge of surface residues helps in locating potential candidates of active sites. Therefore, a method to quickly see the surface residues in a two dimensional model would help to immediately understand the population of amino acid residues on the surface and in the inner core of the proteins. Results: ASA View is an algorithm, an application and a database of schematic representations of solvent accessibility of amino acid residues within proteins. A characteristic two-dimensional spiral plot of solvent accessibility provides a convenient graphical view of residues in terms of their exposed surface areas. In addition, sequential plots in the form of bar charts are also provided. Online plots of the proteins included in the entire Protein Data Bank (PDB), are provided for the entire protein as well as their chains separately. Conclusions: These graphical plots of solvent accessibility are likely to provide a quick view of the overall topological distribution of residues in proteins. Chain-wise computation of solvent accessibility is also provided.
引用
收藏
页数:5
相关论文
共 29 条
[1]   Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information [J].
Ahmad, S ;
Gromiha, MM ;
Sarai, A .
BIOINFORMATICS, 2004, 20 (04) :477-486
[2]   RVP-net: online prediction of real valued accessible surface area of proteins from single sequences [J].
Ahmad, S ;
Gromiha, MM ;
Sarai, A .
BIOINFORMATICS, 2003, 19 (14) :1849-1851
[3]   Real value prediction of solvent accessibility from amino acid sequence [J].
Ahmad, S ;
Gromiha, MM ;
Sarai, A .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2003, 50 (04) :629-635
[4]   NETASA: neural network based prediction of solvent accessibility [J].
Ahmad, S ;
Gromiha, MM .
BIOINFORMATICS, 2002, 18 (06) :819-824
[5]  
[Anonymous], NACCESS COMP PROGR
[6]   Analysis of catalytic residues in enzyme active sites [J].
Bartlett, GJ ;
Porter, CT ;
Borkakoti, N ;
Thornton, JM .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 324 (01) :105-121
[7]   ProTherm, version 4.0: thermodynamic database for proteins and mutants [J].
Bava, KA ;
Gromiha, MM ;
Uedaira, H ;
Kitajima, K ;
Sarai, A .
NUCLEIC ACIDS RESEARCH, 2004, 32 :D120-D121
[8]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[9]  
Cuff JA, 2000, PROTEINS, V40, P502, DOI 10.1002/1097-0134(20000815)40:3<502::AID-PROT170>3.0.CO
[10]  
2-Q