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X‐ray solution scattering studies of the structural diversity intrinsic to protein ensembles
Author(s) -
Makowski Lee,
Gore David,
Mandava Suneeta,
Minh David,
Park Sanghyun,
Rodi Diane J.,
Fischetti Robert F.
Publication year - 2011
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21631
Subject(s) - small angle x ray scattering , chemistry , scattering , intrinsically disordered proteins , myoglobin , chemical physics , function (biology) , small angle scattering , molecular dynamics , protein structure , crystallography , biological system , statistical physics , physics , computational chemistry , optics , biochemistry , evolutionary biology , biology
It is becoming increasingly clear that characterization of the protein ensemble—the collection of all conformations of which the protein is capable—will be a critical step in developing a full understanding of the linkage between structure, dynamics, and function. X‐ray solution scattering in the small angle (SAXS) and wide‐angle (WAXS) regimes represents an important new window to exploring the behavior of ensembles. The characteristics of the ensemble express themselves in X‐ray solution scattering data in predictable ways. Here we present an overview of the effect that structural diversity intrinsic to protein ensembles has on scattering data. We then demonstrate the observation of these effects in scattering from four molecular systems; myoglobin; ubiquitin; alcohol dehydrogenase; and HIV protease; and demonstrate the modulation of these ensembles by ligand binding, mutation, and environmental factors. The observations are analyzed quantitatively in terms of the average spatial extent of structural fluctuations occurring within these proteins under different experimental conditions. The insights which these analyses support are discussed in terms of the function of the various proteins. © 2011 Wiley Periodicals, Inc. Biopolymers 95: 531–542, 2011.