The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Protein Folding Intermediates: Native-State Hydrogen Exchange
Open accessAbstract
The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.
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Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
[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-citationAre there pathways for protein folding?
Levinthal, C. (1968) · Journal de Chimie Physique · doi:10.1051/jcp/1968650044 · Cited by 1,517
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-citationWolynes, P. G., Onuchic, J. N., & Thirumalai, D. (1995) · Science · doi:10.1126/science.7886447 · Cited by 1,200
INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS
Kim, P. S., & Baldwin, R. L. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.003215 · Cited by 1,135
Hvidt, A., & Nielsen, S. O. (1966) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60129-1 · Cited by 1,122
High-resolution three-dimensional structure of horse heart cytochrome c
Bushnell, G. W., Louie, G. V., & Brayer, G. D. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90200-6 · Cited by 1,056
Cited by
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Palmer, A. G., Kroenke, C. D., & Patrick Loria, J. (2001) · Methods in Enzymology · doi:10.1016/s0076-6879(01)39315-1 · Cited by 938
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
MSMBuilder2: Modeling Conformational Dynamics on the Picosecond to Millisecond Scale
Beauchamp, K. A., Bowman, G. R., Lane, T. J., Maibaum, L., Haque, I. S., & Pande, V. S. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200463m · Cited by 372
Simple few-state models reveal hidden complexity in protein folding
Beauchamp, K. A., McGibbon, R., Lin, Y.-S., & Pande, V. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201810109 · Cited by 161
Metadata
- Authors
- Bai, Y., Sosnick, T. R., Mayne, L., & Englander, S. W.
- Venue
- Science
- Published
- 1995-07-14
- Volume
- 269
- Issue
- 5221
- Pages
- 192-197
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2060528711
- Cited by
- 990
- References
- 33
- FWCI
- 14.92
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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