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BIBM
2007
IEEE
104views Bioinformatics» more  BIBM 2007»
13 years 9 months ago
A Protocol to Detect Local Affinities Involved in Proteins Distant Interactions
The tridimensional structure of a protein is constrained or stabilized by some local interactions between distant residues of the protein, such as disulfide bonds, electrostatic i...
Christophe Nicolas Magnan, Cécile Capponi, ...
NAR
2006
120views more  NAR 2006»
13 years 5 months ago
TreeDomViewer: a tool for the visualization of phylogeny and protein domain structure
Phylogenetic analysis and examination of protein domains allow accurate genome annotation and are invaluable to study proteins and protein complex evolution. However, two sequence...
Blaise T. F. Alako, Daphne Rainey, Harm Nijveen, J...
BMCBI
2004
150views more  BMCBI 2004»
13 years 5 months ago
Inter-residue distances derived from fold contact propensities correlate with evolutionary substitution costs
Background: The wealth of information on protein structure has led to a variety of statistical analyses of the role played by individual amino acid types in the protein fold. In p...
Gareth Williams, Patrick Doherty
BMCBI
2006
130views more  BMCBI 2006»
13 years 5 months ago
Docking protein domains in contact space
Background: Many biological processes involve the physical interaction between protein domains. Understanding these functional associations requires knowledge of the molecular str...
Stefano Lise, Alice Walker-Taylor, David T. Jones
JCC
2011
154views more  JCC 2011»
12 years 8 months ago
Can we trust docking results? Evaluation of seven commonly used programs on PDBbind database
: Docking is one of the most commonly used techniques in drug design. It is used for both identifying correct poses of a ligand in the binding site of a protein as well as for the ...
Dariusz Plewczynski, Michal Lazniewski, Rafal Augu...