Changes in lysozyme flexibility upon mutation are frequent, large and long-ranged

PLoS Computational Biology

Volumn 8, Issue 3, 2012, Pages

  Verma, Deeptak ^a   Jacobs, Donald J ^b   Livesay, Dennis R ^a  

^a University of North Carolina at Charlotte   (United States)

^b UNIVERSITY OF NORTH CAROLINA AT CHARLOTTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONSTRAINTS MODELS; COOPERATIVITY; DISTANCE CONSTRAINTS; FLEXIBILITY INDEX; HEN EGG WHITE LYSOZYME; MECHANICAL COUPLING; ORTHOLOGS; SEQUENCE IDENTITY; STATISTICAL MECHANICAL TREATMENT; SUBDOMAIN;

ENZYMES;

AMYLOID; LYSOZYME;

AMINO ACID SUBSTITUTION; ARTICLE; BETA CHAIN; ENZYME ACTIVE SITE; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE SEQUENCE; GENETIC DISTANCE; GENETIC IDENTIFICATION; GENETIC SELECTION; HUMAN; HUMAN VERSUS ANIMAL COMPARISON; MOLECULAR DYNAMICS; ORTHOLOGY; POINT MUTATION; PROTEIN UNFOLDING; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

EID: 84861149876     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002409     Document Type: Article

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