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.

CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology / Paiardini, Alessandro; Bossa, Francesco; Pascarella, Stefano. - In: NUCLEIC ACIDS RESEARCH. - ISSN 0305-1048. - STAMPA. - 33:Web Server Issue(2005), pp. 50-55. [10.1093/nar/gki416]

CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology

PAIARDINI, ALESSANDRO;BOSSA, Francesco;PASCARELLA, Stefano
2005

Abstract

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.
2005
CAMPO; SCR_FIND; CHC_FIND; Protein Structure; Protein evolution; structurally conserved regions; hydrophobic contacts
01 Pubblicazione su rivista::01a Articolo in rivista
CAMPO, SCR_FIND and CHC_FIND: a suite of web tools for computational structural biology / Paiardini, Alessandro; Bossa, Francesco; Pascarella, Stefano. - In: NUCLEIC ACIDS RESEARCH. - ISSN 0305-1048. - STAMPA. - 33:Web Server Issue(2005), pp. 50-55. [10.1093/nar/gki416]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/235852
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