Hydrogen bonding stabilizes globular proteins

Myers, J.K.; Pace, C.N.

doi:10.1016/s0006-3495(96)79401-8

Cited by 308Protein Structure and DynamicsCrystallography and molecular interactionsProtein purification and stability

Hydrogen bonding stabilizes globular proteins

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Myers, J.K., Pace, C.N.·1996·Biophysical Journal

DOI 10.1016/s0006-3495(96)79401-8PMC PMC1233669

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Abstract

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, but they lack the ability to form regular repeating intramolecular hydrogen bonding motifs that facilitate protein folding.
“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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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)
DOI: 10.1016/s0006-3495(96)79401-8
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6132 d)
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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Hydrogen bonding stabilizes globular proteins

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