The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Protein stability parameters measured by hydrogen exchange
Abstract
The hydrogen exchange (HX) rates of the slowest peptide group NH hydrogens in oxidized cytochrome c (equine) are controlled by the transient global unfolding equilibrium. These rates can be measured by one‐dimensional nuclear magnetic resonance and used to determine the thermodynamic parameters of global unfolding at mild solution conditions well below the melting transition. The free energy for global unfolding measured by hydrogen exchange can differ from values found by standard denaturation methods, most notably due to the slow cis‐trans isomerization of the prolyl peptide bond. This difference can be quantitatively calculated from basic principles. Even with these corrections, HX experiments at low denaturant concentration measure a free energy of protein stability that rises above the usual linear extrapolation from denaturation data, as predicted by the denaturant binding model of Tanford. © 1994 Wiley‐Liss, Inc.
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Cites
[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
Pace, C. N. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,258
Primary structure effects on peptide group hydrogen exchange
Bai, Y., Milne, J. S., Mayne, L., & Englander, S. W. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170110 · Cited by 1,902
Self-citationPrivalov, P. L., & Khechinashvili, N. N. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90188-0 · Cited by 1,399
Hydrogen exchange and structural dynamics of proteins and nucleic acids
Englander, S. W., & Kallenbach, N. R. (1983) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005217 · Cited by 1,356
Self-citationHvidt, A., & Nielsen, S. O. (1966) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60129-1 · Cited by 1,122
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
Jackson, S. E., & Fersht, A. R. (1991) · Biochemistry · doi:10.1021/bi00107a010 · Cited by 878
Dill, K. A., & Shortle, D. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.004051 · Cited by 874
Protein interactions with urea and guanidinium chloride
Makhatadze, G. I., & Privalov, P. L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90963-k · Cited by 623
The barriers in protein folding
Sosnick, T. R., Mayne, L., Hiller, R., & Englander, S. W. (1994) · Nature Structural Biology · doi:10.1038/nsb0394-149 · Cited by 433
Self-citationIsotope effects in peptide group hydrogen exchange
Connelly, G. P., Bai, Y., Jeng, M., & Englander, S. W. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170111 · Cited by 376
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Cited by
Protein Folding Intermediates: Native-State Hydrogen Exchange
Bai, Y., Sosnick, T. R., Mayne, L., & Englander, S. W. (1995) · Science · doi:10.1126/science.7618079 · Cited by 990
Self-citationDo enthalpy and entropy distinguish first in class from best in class?
Freire, E. (2008) · Drug Discovery Today · doi:10.1016/j.drudis.2008.07.005 · Cited by 491
Mechanisms and uses of hydrogen exchange
Englander, S. W., Sosnick, T. R., Englander, J. J., & Mayne, L. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80090-x · Cited by 383
Self-citationInfrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz-Fonfria, V. A. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 325
Protein folding: The stepwise assembly of foldon units
Maity, H., Maity, M., Krishna, M. M. G., Mayne, L., & Englander, S. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501043102 · Cited by 300
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Metadata
- Authors
- Bai, Y., Milne, J. S., Mayne, L., & Englander, S. W.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 1994-09
- Volume
- 20
- Issue
- 1
- Pages
- 4-14
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W1994530375
- Cited by
- 307
- References
- 28
- FWCI
- 4.53
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bai, Y., Milne, J. S., Mayne, L., & Englander, S. W. (1994). Protein stability parameters measured by hydrogen exchange. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340200103
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