Role of cavities and hydration in the pressure unfolding of T4lysozyme

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

Volumn 111, Issue 38, 2014, Pages 13846-13851

  Nucci, Nathaniel V ^a,b   Fuglestad, Brian ^a   Athanasoula, Evangelia A ^a   Wand, A Joshua ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b ROWAN UNIVERSITY   (United States)

Author keywords

High pressure NMR; Protein folding and cooperativity; Protein hydration; Protein stability; Reverse micelle encapsulation

Indexed keywords

LYSOZYME;

AMINO ACID SUBSTITUTION; CHEMICAL PHENOMENA; CHEMISTRY; ENTEROBACTERIA PHAGE T4; ENZYMOLOGY; GENETICS; MISSENSE MUTATION; PRESSURE; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING;

AMINO ACID SUBSTITUTION; BACTERIOPHAGE T4; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MURAMIDASE; MUTATION, MISSENSE; PRESSURE; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING;

EID: 84907192008     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1410655111     Document Type: Article

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