Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein

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

Volumn 111, Issue 32, 2014, Pages 11685-11690

  Robinson, Aaron C ^a   Castañeda, Carlos A ^a   Schlessman, Jamie L ^a,b   Bertrand Garcia Moreno E ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNITED STATES NAVAL ACADEMY   (United States)

Author keywords

Dielectric constant; Electrostatics; Enzyme design; Internal charge; Low barrier hydrogen bond

Indexed keywords

ION; PROTEIN; WATER;

ARTICLE; CHEMICAL ENVIRONMENT; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; DIELECTRIC CONSTANT; DIPOLE; FLUORESCENCE; HYDROGEN BOND; HYDROPHOBICITY; MICROENVIRONMENT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN INTERACTION; PROTEIN STRUCTURE; THERMODYNAMICS;

DIELECTRIC CONSTANT; ELECTROSTATICS; ENZYME DESIGN; INTERNAL CHARGE; LOW-BARRIER HYDROGEN BOND;

AMINO ACID SUBSTITUTION; BIOPHYSICAL PHENOMENA; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; IONS; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEINS; RECOMBINANT PROTEINS; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 84905968919     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1402900111     Document Type: Article

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