CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology.
The identification of evolutionarily conserved features of protein structures can provide insights into their functional and structural properties. Three methods have been developed and implemented as WWW tools, CAMPO, SCR_FIND and CHC_FIND, to analyze evolutionarily conserved residues (ECRs), structurally conserved regions (SCRs) and conserved hydrophobic contacts (CHCs) in protein families and superfamilies, on the basis of their 3D structures and the homologous sequences available. The programs identify protein segments that conserve a similar main-chain conformation, compute residue-to-residue hydrophobic contacts involving only apolar atoms common to all the 3D structures analyzed and allow the identification of conserved amino-acid sites among protein structures and their homologous sequences. The programs also allow the visualization of SCRs, CHCs and ECRs directly on the superposed structures and their multiple structural and sequence alignments. Tools and tutorials explaining their usage are available at http://schubert.bio.uniroma1.it/SCR_FIND, http://schubert.bio.uniroma1.it/CHC_FIND and http://schubert.bio.uniroma1.it/CAMPO.
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Università La Sapienza, Piazzale Aldo Moro 5, 00185 Roma, Italy.
Alessandro
A
Paiardini
Francesco
F
Bossa
Stefano
S
Pascarella
D019295:Computational Biology; D019143:Evolution, Molecular; D057927:Hydrophobic and Hydrophilic Interactions; D020407:Internet; D008958:Models, Molecular; D015221:Potassium Channels / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D012984:Software; D014361:Trypsin Inhibitors / Q000737:chemistry
D015221:Potassium Channels; D011506:Proteins; D014361:Trypsin Inhibitors