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Structure and dynamics of the water around myoglobin
Author(s) -
Phillips George N.,
Montgomery Pettitt B.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040202
Subject(s) - myoglobin , solvation , observable , chemical physics , protein dynamics , molecular dynamics , chemistry , function (biology) , dynamics (music) , solvent , computational chemistry , thermodynamics , physics , biology , biochemistry , quantum mechanics , evolutionary biology , acoustics
Abstract The interplay between simulations at various levels of hydration and experimental observables has led to a picture of the role of solvent in thermodynamics and dynamics of protein systems. One of the most studied protein‐solvent systems is myoglobin, which serves as a paradigm for the development of structure‐function relationships in many biophysical studies. We review here some aspects of the solvation of myoglobin and the resulting implications. In particular, recent theoretical and simulation studies unify much of the diverse set of experimental results on water near proteins.