NIAS-Server: Neighbors Influence of Amino acids and Secondary Structures in Proteins

被引:18
作者
Borguesan, Bruno [1 ]
Inostroza-Ponta, Mario [2 ]
Dorn, Marcio [1 ]
机构
[1] Univ Fed Rio Grande do Sul, Inst Informat, Ave Bento Goncalves 9500, BR-91501970 Porto Alegre, RS, Brazil
[2] Univ Santiago Chile, Dept Ingn Informat, Ctr Biotechnol & Bioengn, Santiago, Chile
关键词
conformational preferences; three-dimensional structure of proteins; structural biology; STRUCTURE PREDICTION; DATA-BANK; SEQUENCE; MOTIFS; CONFORMATION; PATTERN; LOOPS;
D O I
10.1089/cmb.2016.0074
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The exponential growth in the number of experimentally determined three-dimensional protein structures provide a new and relevant knowledge about the conformation of amino acids in proteins. Only a few of probability densities of amino acids are publicly available for use in structure validation and prediction methods. NIAS (Neighbors Influence of Amino acids and Secondary structures) is a web-based tool used to extract information about conformational preferences of amino acid residues and secondary structures in experimental-determined protein templates. This information is useful, for example, to characterize folds and local motifs in proteins, molecular folding, and can help the solution of complex problems such as protein structure prediction, protein design, among others. The NIAS-Server and supplementary data are available at http://sbcb.inf.ufrgs.br/nias.
引用
收藏
页码:255 / 265
页数:11
相关论文
共 48 条
[31]   CASP10 results compared to those of previous CASP experiments [J].
Kryshtafovych, Andriy ;
Fidelis, Krzysztof ;
Moult, John .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2014, 82 :164-174
[32]  
Liljas A., 2016, Textbook of structural biology
[33]   Protein secondary structure assignment revisited: a detailed analysis of different assignment methods [J].
Martin, J ;
Letellier, G ;
Marin, A ;
Taly, JF ;
de Brevern, AG ;
Gibrat, JF .
BMC STRUCTURAL BIOLOGY, 2005, 5
[34]   APDbase: Amino acid Physico-chemical properties Database [J].
Mathura, Venkatarajan S. ;
Kolippakkam, Deepak .
BIOINFORMATION, 2005, 1 (01) :2-4
[35]   Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins [J].
Moelbert, S ;
Emberly, E ;
Tang, C .
PROTEIN SCIENCE, 2004, 13 (03) :752-762
[36]   LOGICAL ANALYSIS OF MECHANISM OF PROTEIN FOLDING .1. PREDICTIONS OF HELICES, LOOPS AND BETA-STRUCTURES FROM PRIMARY STRUCTURE [J].
NAGANO, K .
JOURNAL OF MOLECULAR BIOLOGY, 1973, 75 (02) :401-420
[37]   THE PLEATED SHEET, A NEW LAYER CONFIGURATION OF POLYPEPTIDE CHAINS [J].
PAULING, L ;
COREY, RB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1951, 37 (05) :251-256
[38]   THE STRUCTURE OF PROTEINS - 2 HYDROGEN-BONDED HELICAL CONFIGURATIONS OF THE POLYPEPTIDE CHAIN [J].
PAULING, L ;
COREY, RB ;
BRANSON, HR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1951, 37 (04) :205-211
[39]   Amino acid neighbours and detailed conformational analysis of cysteines in proteins [J].
Petersen, MTN ;
Jonson, PH ;
Petersen, SB .
PROTEIN ENGINEERING, 1999, 12 (07) :535-548
[40]   IDENTIFICATION OF STRUCTURAL MOTIFS FROM PROTEIN COORDINATE DATA - SECONDARY STRUCTURE AND 1ST-LEVEL SUPERSECONDARY STRUCTURE [J].
RICHARDS, FM ;
KUNDROT, CE .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1988, 3 (02) :71-84