Geofold: Topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 3, 2012, Pages 920-934

  Ramakrishnan, Vibin ^a,b,e   Srinivasan, Sai Praveen ^a,c   Salem, Saeed M ^d,g   Matthews, Suzanne J ^d,f   Colón, Wilfredo ^a,c   Zaki, Mohammed ^d   Bystroff, C ^a,b,d  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^c Research Rensselaer Polytechnic Institute   (United States)

^d Rensselaer Polytechnic Institute   (United States)

^e INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

^f North Dakota State University   (United States)

^g Texas AandM University   (United States)

Author keywords

Barnase; Configurational entropy; DHFR; Kinetic stability; Lysozyme FIS; Pathways; Topology

Indexed keywords

BARNASE; DIHYDROFOLATE REDUCTASE; DISULFIDE; LYSOZYME;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENTROPY; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING;

BACILLUS; BACTERIOPHAGE T4; DISULFIDES; ENTROPY; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MURAMIDASE; MUTATION; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN UNFOLDING; PROTEINS; RIBONUCLEASES; SOFTWARE; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 84856779614     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23249     Document Type: Article

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