A Case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1

Methods in Molecular Biology

Volumn 1084, Issue , 2014, Pages 227-238

  Brown, Matthew C ^a   Verma, Deeptak ^a   Russell, Christian ^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

Allostery; Distance constraint model; Protein flexibility; Quantitative stability flexibility relationships; Lactamase

Indexed keywords

ENZYME; METALLO BETA LACTAMASE; NDM 1 ENZYME; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; CASE STUDY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; KLEBSIELLA PNEUMONIAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RIGIDITY; SEQUENCE ALIGNMENT;

KLEBSIELLA PNEUMONIAE;

BETA-LACTAMASES; MODELS, MOLECULAR; PROTEIN STABILITY; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 84934436146     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-658-0_12     Document Type: Article

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