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Hydrogen exchange and structural dynamics of proteins and nucleic acids
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( —Gi/RT) for each state of free energy Gi(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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Citations
Cited by
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129
“Thus every encounter of an acidic side chain group with OH − will abstract the side chain proton while on average 1000 collisions are needed to deprotonate an amide group [250].”
BackgroundInfluentialThe Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Chemical exchange saturation transfer (CEST): what is in a name and what isn't?
van Zijl, P. C. M., & Yadav, N. N. (2011) · Magnetic Resonance in Medicine · doi:10.1002/mrm.22761 · Cited by 1,155
A Buried Polar Interaction Imparts Structural Uniqueness in a Designed Heterodimeric Coiled Coil
Lumb, K. J., & Kim, P. S. (1995) · Biochemistry · doi:10.1021/bi00027a013 · Cited by 266
Ligand binding to proteins: The binding landscape model
Miller, D. W., & Dill, K. A. (1997) · Protein Science · doi:10.1002/pro.5560061011 · Cited by 178
Metadata
- Authors
- Englander, S. W., & Kallenbach, N. R.
- Venue
- Quarterly Reviews of Biophysics
- Publisher
- Cambridge University Press (CUP)
- Published
- 1983-11
- Volume
- 16
- Issue
- 4
- Pages
- 521-655
- ISSN
- 0033-5835 (ISSN-L)
- 1469-8994
- OpenAlex
- W2062972508
- Cited by
- 1,356
- References
- 0
- FWCI
- 3.61
- Type
- journal article
- Language
- en
- Open access
- closed
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- Englander, S. W., & Kallenbach, N. R. (1983). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Reviews of Biophysics. https://doi.org/10.1017/s0033583500005217
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