Current Protocols in Protein Science · 2007 · 2.9K citations · 216 references
Life SciencesBioinformaticsBiologyComputational BiologyStructural BioinformaticsStructural BiologyComparative ModelingHomology ModelingProtein Sequence AnalysisProtein StructureProtein Structure ModelingTemplate-based ModelingFold AssignmentFold MappingModel Performance EvaluationPredictionProtein Structure ComparisonTarget-template AlignmentTemplate-based Model EvaluationTemplate-based Protein Structure Prediction
Functional characterization of a protein sequence is a common goal in biology, and is usually facilitated by having an accurate three-dimensional (3-D) structure of the studied protein. In the absence of an experimentally determined structure, comparative or homology modeling can sometimes provide a useful 3-D model for a protein that is related to at least one known protein structure. Comparative modeling predicts the 3-D structure of a given protein sequence (target) based primarily on its alignment to one or more proteins of known structure (templates). The prediction process consists of fold assignment, target-template alignment, model building, and model evaluation. This unit describes how to calculate comparative models using the program MODELLER and discusses all four steps of comparative modeling, frequently observed errors, and some applications. Modeling lactate dehydrogenase from Trichomonas vaginalis (TvLDH) is described as an example. The download and installation of the MODELLER software is also described.
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Julie Thompson, Desmond G. Higgins, Toby J. Gibson · Nucleic Acids Research · 1994 · 64.9K citations · Full text
MUSCLE: multiple sequence alignment with high accuracy and high throughput
R. C. Edgar · Nucleic Acids Research · 2004 · 46.5K citations · Full text
Helen M. Berman · Nucleic Acids Research · 2000 · 39.8K citations
PHYLIP-Phylogeny inference package (Version 3.2)
Joe Felsenstein · Cladistics · 1989 · 17.9K citations