The DOI matches its Crossref record; 72 of the 74 references it cites were found in a registry or an index.
Hydrogen bonding stabilizes globular proteins
Open accessAbstract
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globular proteins. It is not clear, however, whether they make a net favorable contribution to this stability. Experimental and theoretical studies are at odds over this important question. Measurements of the change in conformational stability, delta (delta G), for the mutation of a hydrogen bonded residue to one incapable of hydrogen bonding suggest a stabilization of 1.0 kcal/mol per hydrogen bond. If the delta (delta G) values are corrected for differences in side-chain hydrophobicity and conformational entropy, then the estimated stabilization becomes 2.2 kcal/mol per hydrogen bond. These and other experimental studies discussed here are consistent and compelling: hydrogen bonding stabilizes globular proteins.
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“Polyester systems can interact due to hydrophilic, hydrophobic, and electrostatic interactions such as dipole-dipole interactions [41], but they lack the ability to form regular repeating intramolecular hydrogen bonding motifs of the sort that facilitate protein folding [42,43].”
From Polyesters as a Model System for Building Primitive Biologies from Non-Biological Prebiotic Chemistry (2020) · cites this paper as [43]
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Protein Structure and the Energetics of Protein Stability
Robertson, A. D., & Murphy, K. P. (1997) · Chemical Reviews · doi:10.1021/cr960383c · Cited by 683
Contribution of hydrogen bonds to protein stability
Pace, C. N., Fu, H., Fryar, K. L., Landua, J. D., Trevino, S. R., Schell, D., Thurlkill, R. L., Imura, S., Scholtz, J. M., Gajiwala, K. S., et al. (2014) · Protein Science · doi:10.1002/pro.2449 · Cited by 599
Self-citationA backbone-based theory of protein folding
Rose, G. D., Fleming, P. J., Banavar, J. R., & Maritan, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606843103 · Cited by 480
Contribution of Hydrophobic Interactions to Protein Stability
Pace, C. N., Fu, H., Fryar, K. L., Landua, J. D., Trevino, S. R., Shirley, B. A., McNutt, M., Iimura, S., Gajiwala, K. S., Scholtz, J. M., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.053 · Cited by 460
Self-citationProtein structure, stability and solubility in water and other solvents
Pace, C. N., Trevino, S. R., Prabhakaran, E. N., & Scholtz, J. M. (2004) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2004.1500 · Cited by 395
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Metadata
- Authors
- Myers, J. K., & Pace, C. N.
- Affiliations
- Texas A&M University (US)
- ORCID
- Pace, C.N.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 1996-10
- Volume
- 71
- Issue
- 4
- Pages
- 2033-2039
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC1233669
- OpenAlex
- W2025925640
- Cited by
- 308
- References
- 74
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 11 · 2022: 12 · 2021: 8 · 2020: 8 · 2019: 7 · 2018: 9 · 2017: 11 · 2016: 11 · 2015: 8 · 2014: 11 · 2013: 8 · 2012: 8
- FWCI
- 4.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM008523, GM37039, T32 GM 08523, R01GM037039)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Crystallography and molecular interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- hydrogen bonding, protein stability, globular proteins, intramolecular hydrogen bonding, conformational stability, side chain hydrophobicity, conformational entropy
- MeSH terms
- Calorimetry, Hydrogen Bonding, Micrococcal Nuclease, Models, Theoretical, Muramidase, Protein Conformation, Protein Denaturation, Proteins, Recombinant Proteins, Thermodynamics, Mutagenesis, Site-Directed, Bacteriophage T4, Point Mutation
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