Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 13, 2012, Pages 4857-4862

  Bershtein, Shimon ^a   Wu, Wanmeng ^a,b   Shakhnovich, Eugene I ^a  

^a HARVARD UNIVERSITY   (United States)

^b JIANGNAN UNIVERSITY   (China)

Author keywords

Fitness landscape; Genotype phenotype relation; Molecular evolution; Protein aggregation; Protein solubility

Indexed keywords

DIHYDROFOLATE REDUCTASE;

ARTICLE; BACTERIAL STRAIN; CATALYSIS; CONTROLLED STUDY; CORRELATION ANALYSIS; CULTURE MEDIUM; ESCHERICHIA COLI; FITNESS; FOLA GENE; GENE; HOMEOSTASIS; HUMAN; MUTANT; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; WILD TYPE;

CHROMOSOMES, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC FITNESS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; PROTEIN STRUCTURE, QUATERNARY; SOLUBILITY; TEMPERATURE; TETRAHYDROFOLATE DEHYDROGENASE;

ESCHERICHIA COLI;

EID: 84859476261     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1118157109     Document Type: Article

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