Hydrogen exchange and structural dynamics of proteins and nucleic acids

1983/11/01 by S. Walter Englander, Neville R. Kallenbach · 1,361 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Biochemistry #Chemical physics #Chemistry #Crystallography #DNA and Nucleic Acid Chemistry #Enzyme Structure and Function #Macromolecule #Molecule #Native state #Nucleic acid #Population #Protein Structure and Dynamics

paper · doi:10.1017/s0033583500005217

published in Quarterly Reviews of Biophysics 16(4), 521-655 (Cambridge University Press)

openalex publication_date 1983/11/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30

Abstract

Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid. Most structural work to date has centred upon the native state of macromolecules, the most probable macromolecular form. But the native state of a molecule is merely its most abundant form, certainly not its only form. Thermodynamics requires that all other possible structural forms, however improbable, must also exist, albeit with representation corresponding to the factor exp( — G i / RT ) for each state of free energy G i (see Moelwyn-Hughes, 1961), and one appreciates that each molecule within a population of molecules will in time explore the vast ensemble of possible structural states.

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