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BIOINFORMATICS
2011
12 years 11 months ago
A method for probing the mutational landscape of amyloid structure
Motivation: Proteins of all kinds can self-assemble into highly ordered β-sheet aggregates known as amyloid fibrils, important both biologically and clinically. However, the spe...
Charles W. O'Donnell, Jérôme Waldisp&...
BMCBI
2006
137views more  BMCBI 2006»
13 years 7 months ago
A maximum likelihood framework for protein design
Background: The aim of protein design is to predict amino-acid sequences compatible with a given target structure. Traditionally envisioned as a purely thermodynamic question, thi...
Claudia L. Kleinman, Nicolas Rodrigue, Céci...
BMCBI
2008
176views more  BMCBI 2008»
13 years 7 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
2004
177views more  BMCBI 2004»
13 years 7 months ago
Gapped alignment of protein sequence motifs through Monte Carlo optimization of a hidden Markov model
Background: Certain protein families are highly conserved across distantly related organisms and belong to large and functionally diverse superfamilies. The patterns of conservati...
Andrew F. Neuwald, Jun S. Liu
BMCBI
2005
105views more  BMCBI 2005»
13 years 7 months ago
Secondary structure assignment that accurately reflects physical and evolutionary characteristics
Background: Secondary structure is used in hierarchical classification of protein structures, identification of protein features, such as helix caps and loops, for fold recognitio...
Maria Vittoria Cubellis, Fabien Cailliez, Simon C....