» Articles » PMID: 15215352

CRASP: a Program for Analysis of Coordinated Substitutions in Multiple Alignments of Protein Sequences

Overview
Specialty Biochemistry
Date 2004 Jun 25
PMID 15215352
Citations 18
Authors
Affiliations
Soon will be listed here.
Abstract

Recent results suggest that during evolution certain substitutions at protein sites may occur in a coordinated manner due to interactions between amino acid residues. Information on these coordinated substitutions may be useful for analysis of protein structure and function. CRASP is an Internet-available software tool for the detection and analysis of coordinated substitutions in multiple alignments of protein sequences. The approach is based on estimation of the correlation coefficient between the values of a physicochemical parameter at a pair of positions of sequence alignment. The program enables the user to detect and analyze pairwise relationships between amino acid substitutions at protein sequence positions, estimate the contribution of the coordinated substitutions to the evolutionary invariance or variability in integral protein physicochemical characteristics such as the net charge of protein residues and hydrophobic core volume. The CRASP program is available at http://wwwmgs.bionet.nsc.ru/mgs/programs/crasp/.

Citing Articles

Enhanced thermal stability enables human mismatch-specific thymine-DNA glycosylase to catalyse futile DNA repair.

Manapkyzy D, Joldybayeva B, Ishchenko A, Matkarimov B, Zharkov D, Taipakova S PLoS One. 2024; 19(10):e0304818.

PMID: 39423202 PMC: 11488719. DOI: 10.1371/journal.pone.0304818.


LARGE-SCALE MULTIPLE INFERENCE OF COLLECTIVE DEPENDENCE WITH APPLICATIONS TO PROTEIN FUNCTION.

Jernigan R, Jia K, Ren Z, Zhou W Ann Appl Stat. 2022; 15(2):902-924.

PMID: 35910493 PMC: 9337751. DOI: 10.1214/20-aoas1431.


SubVis: an interactive R package for exploring the effects of multiple substitution matrices on pairwise sequence alignment.

Barlowe S, Coan H, Youker R PeerJ. 2017; 5:e3492.

PMID: 28674656 PMC: 5490468. DOI: 10.7717/peerj.3492.


Origins and evolution of WUSCHEL-related homeobox protein family in plant kingdom.

Lian G, Ding Z, Wang Q, Zhang D, Xu J ScientificWorldJournal. 2014; 2014:534140.

PMID: 24511289 PMC: 3913392. DOI: 10.1155/2014/534140.


Janus: prediction and ranking of mutations required for functional interconversion of enzymes.

Addington T, Mertz R, Siegel J, Thompson J, Fisher A, Filkov V J Mol Biol. 2013; 425(8):1378-89.

PMID: 23396064 PMC: 3615137. DOI: 10.1016/j.jmb.2013.01.034.


References
1.
Afonnikov D, Oshchepkov D, Kolchanov N . Detection of conserved physico-chemical characteristics of proteins by analyzing clusters of positions with co-ordinated substitutions. Bioinformatics. 2001; 17(11):1035-46. DOI: 10.1093/bioinformatics/17.11.1035. View

2.
Nagl S . Can correlated mutations in protein domain families be used for protein design?. Brief Bioinform. 2001; 2(3):279-88. DOI: 10.1093/bib/2.3.279. View

3.
Eisenberg D, Weiss R, Terwilliger T . The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature. 1982; 299(5881):371-4. DOI: 10.1038/299371a0. View

4.
Vingron M, Argos P . A fast and sensitive multiple sequence alignment algorithm. Comput Appl Biosci. 1989; 5(2):115-21. DOI: 10.1093/bioinformatics/5.2.115. View

5.
Kimura M . Recent development of the neutral theory viewed from the Wrightian tradition of theoretical population genetics. Proc Natl Acad Sci U S A. 1991; 88(14):5969-73. PMC: 52003. DOI: 10.1073/pnas.88.14.5969. View