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Protein structure prediction from sequence variation
by
Hopf, Thomas A
, Sander, Chris
, Marks, Debora S
in
631/114/2411
/ 631/61/475
/ Agriculture
/ Amino Acid Sequence
/ Amino acids
/ Bioinformatics
/ Biomedical Engineering/Biotechnology
/ Biomedicine
/ Biotechnology
/ Computer Simulation
/ Evolutionary biology
/ Genetic Variation - genetics
/ Life Sciences
/ Models, Chemical
/ Models, Genetic
/ Models, Molecular
/ Molecular Sequence Data
/ perspective
/ Phylogenetics
/ Protein Conformation
/ Proteins
/ Proteins - chemistry
/ Proteins - genetics
/ Residues
/ Sequence Analysis, Protein - methods
/ Statistical methods
2012
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Protein structure prediction from sequence variation
by
Hopf, Thomas A
, Sander, Chris
, Marks, Debora S
in
631/114/2411
/ 631/61/475
/ Agriculture
/ Amino Acid Sequence
/ Amino acids
/ Bioinformatics
/ Biomedical Engineering/Biotechnology
/ Biomedicine
/ Biotechnology
/ Computer Simulation
/ Evolutionary biology
/ Genetic Variation - genetics
/ Life Sciences
/ Models, Chemical
/ Models, Genetic
/ Models, Molecular
/ Molecular Sequence Data
/ perspective
/ Phylogenetics
/ Protein Conformation
/ Proteins
/ Proteins - chemistry
/ Proteins - genetics
/ Residues
/ Sequence Analysis, Protein - methods
/ Statistical methods
2012
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Do you wish to request the book?
Protein structure prediction from sequence variation
by
Hopf, Thomas A
, Sander, Chris
, Marks, Debora S
in
631/114/2411
/ 631/61/475
/ Agriculture
/ Amino Acid Sequence
/ Amino acids
/ Bioinformatics
/ Biomedical Engineering/Biotechnology
/ Biomedicine
/ Biotechnology
/ Computer Simulation
/ Evolutionary biology
/ Genetic Variation - genetics
/ Life Sciences
/ Models, Chemical
/ Models, Genetic
/ Models, Molecular
/ Molecular Sequence Data
/ perspective
/ Phylogenetics
/ Protein Conformation
/ Proteins
/ Proteins - chemistry
/ Proteins - genetics
/ Residues
/ Sequence Analysis, Protein - methods
/ Statistical methods
2012
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Journal Article
Protein structure prediction from sequence variation
2012
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Overview
Genomic sequences contain rich evolutionary information about functional constraints on macromolecules such as proteins. This information can be efficiently mined to detect evolutionary couplings between residues in proteins and address the long-standing challenge to compute protein three-dimensional structures from amino acid sequences. Substantial progress has recently been made on this problem owing to the explosive growth in available sequences and the application of global statistical methods. In addition to three-dimensional structure, the improved understanding of covariation may help identify functional residues involved in ligand binding, protein-complex formation and conformational changes. We expect computation of covariation patterns to complement experimental structural biology in elucidating the full spectrum of protein structures, their functional interactions and evolutionary dynamics.
Publisher
Nature Publishing Group US,Nature Publishing Group
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