Inactive conformation enhances binding function in physiological conditions

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

Volumn 112, Issue 32, 2015, Pages 9884-9889

  Yakovenko, Olga ^a   Tchesnokova, Veronika ^a   Sokurenko, Evgeni V ^a   Thomas, Wendy E ^a   Springer, Timothy A ^b  

^a UNIVERSITY OF WASHINGTON   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Adhesion; Conformational dynamics; Ligand; Mechanical force; Receptor

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; FIMH PROTEIN; FOCH PROTEIN; K12 PROTEIN; MANNOSE; PROTEIN VARIANT; UNCLASSIFIED DRUG; BOVINE SERUM ALBUMIN; FIMBRIA PROTEIN; FIMH PROTEIN, E COLI; MUTANT PROTEIN; PROTEIN BINDING;

ARTICLE; BACTERIUM ADHERENCE; BINDING AFFINITY; BINDING KINETICS; CELL ADHESION; CONFORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; ANIMAL; ATOMIC FORCE MICROSCOPY; BIOMECHANICS; BOVINE; CHEMICAL STRUCTURE; CHEMISTRY; FIMBRIA; FLOW KINETICS; KINETICS; METABOLISM; PHYSIOLOGY; PROTEIN CONFORMATION; TIME;

BACTERIA (MICROORGANISMS);

ADHESINS, ESCHERICHIA COLI; ANIMALS; BACTERIAL ADHESION; BIOMECHANICAL PHENOMENA; CATTLE; ESCHERICHIA COLI; FIMBRIAE PROTEINS; FIMBRIAE, BACTERIAL; KINETICS; MANNOSE; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; RHEOLOGY; SERUM ALBUMIN, BOVINE; TIME FACTORS;

EID: 84938939972     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1503160112     Document Type: Article

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