Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure

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

Volumn 112, Issue 19, 2015, Pages E2437-E2446

  Lerch, Michael T ^a,b   López, Carlos J ^a,b,c   Yang, Zhongyu ^a,b   Kreitman, Margaux J ^a,b   Horwitz, Joseph ^a   Hubbell, Wayne L ^a,b  

^a JULES STEIN EYE INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Grifols SA   (United States)

Author keywords

Conformational exchange; DEER; EPR; Protein structural dynamics

Indexed keywords

LYSOZYME; LIGAND; SOLVENT;

ARTICLE; CIRCULAR DICHROISM; ELECTRON; HYDRATION; HYDROSTATIC PRESSURE; MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SPIN LABELING; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON SPIN RESONANCE; ENTEROBACTERIA PHAGE T4; ENZYMOLOGY; GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PROTEIN DENATURATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TEMPERATURE; THERMODYNAMICS;

BACTERIOPHAGE T4; CIRCULAR DICHROISM; ELECTRON SPIN RESONANCE SPECTROSCOPY; HYDROGEN-ION CONCENTRATION; HYDROSTATIC PRESSURE; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MURAMIDASE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; THERMODYNAMICS;

EID: 84929164097     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1506505112     Document Type: Article

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