Computational Protein Design Quantifies Structural Constraints on Amino Acid Covariation

PLoS Computational Biology

Volumn 9, Issue 11, 2013, Pages

  Ollikainen, Noah ^a   Kortemme, Tanja ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; STRUCTURAL DESIGN;

AMINO-ACIDS; CO-VARIATIONS; COMPUTATIONAL PROTEIN DESIGN; DESIGN METHOD; MULTIPLE FACTORS; NATURALLY OCCURRING; PHYLOGENETICS; PROTEINS STRUCTURES; SELECTIVE PRESSURE; STRUCTURAL CONSTRAINTS;

AMINO ACIDS;

ACCURACY; AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; CALCULATION; COMPUTATIONAL PROTEIN DESIGN; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENTROPY; HYDROGEN BOND; MONTE CARLO METHOD; PREDICTION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SIMULATION;

AMINO ACID SEQUENCE; AMINO ACIDS; COMPUTATIONAL BIOLOGY; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTEINS;

EID: 84888273231     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003313     Document Type: Article

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