Servers for sequence–structure relationship analysis and prediction

AUTOR(ES)

Dosztányi, Zsuzsanna

FONTE

Oxford University Press

RESUMO

We describe several algorithms and public servers that were developed to analyze and predict various features of protein structures. These servers provide information about the covalent state of cysteine (CYSREDOX), as well as about residues involved in non-covalent cross links that play an important role in the structural stability of proteins (SCIDE and SCPRED). We also discuss methods and servers developed to identify helical transmembrane proteins from large databases and rough genomic data, including two of the most popular transmembrane prediction methods, DAS and HMMTOP. Several biologically interesting applications of these servers are also presented. The servers are available through http://www.enzim.hu/servers.html.

Documentos Relacionados

• Protein folding funnels: a kinetic approach to the sequence-structure relationship.
• trilogy: Discovery of sequence–structure patterns across diverse proteins
• Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination.
• Structural characterization of genomes by large scale sequence-structure threading
• The RESID Database of protein structure modifications and the NRL-3D Sequence–Structure Database