Structure and dynamics of the water around myoglobin

George N. Phillips, B. Montgomery Pettitt

Research output: Contribution to journalReview article

82 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)149-158
Number of pages10
JournalProtein Science
Volume4
Issue number2
DOIs
StatePublished - Feb 1995
Externally publishedYes

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Keywords

  • diffraction analysis
  • hydration
  • myoglobin
  • protein solutions
  • solvation
  • water dynamics

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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