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» PROFbval: predict flexible and rigid residues in proteins
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BMCBI
2008
176views more  BMCBI 2008»
13 years 11 months ago
H2r: Identification of evolutionary important residues by means of an entropy based analysis of multiple sequence alignments
Background: A multiple sequence alignment (MSA) generated for a protein can be used to characterise residues by means of a statistical analysis of single columns. In addition to t...
Rainer Merkl, Matthias Zwick
BMCBI
2007
117views more  BMCBI 2007»
13 years 11 months ago
Supervised multivariate analysis of sequence groups to identify specificity determining residues
Background: Proteins that evolve from a common ancestor can change functionality over time, and it is important to be able identify residues that cause this change. In this paper ...
Iain M. Wallace, Desmond G. Higgins
TCBB
2010
104views more  TCBB 2010»
13 years 9 months ago
Fast Hinge Detection Algorithms for Flexible Protein Structures
— Analysis of conformational changes is one of the keys to the understanding of protein functions and interactions. For the analysis, we often compare two protein structures, tak...
Tetsuo Shibuya
BMCBI
2007
113views more  BMCBI 2007»
13 years 11 months ago
Hinge Atlas: relating protein sequence to sites of structural flexibility
Background: Relating features of protein sequences to structural hinges is important for identifying domain boundaries, understanding structure-function relationships, and designi...
Samuel Flores, Long J. Lu, Julie Yang, Nicholas Ca...
BMCBI
2008
124views more  BMCBI 2008»
13 years 11 months ago
Alignment of protein structures in the presence of domain motions
Background: Structural alignment is an important step in protein comparison. Well-established methods exist for solving this problem under the assumption that the structures under...
Roberto Mosca, Barbara Brannetti, Thomas R. Schnei...