Cited by 73Protein Structure and DynamicsCrystallography and molecular interactionsEnzyme Structure and Function

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The Role of Side-chain Hydrogen Bonds in the Formation and Stabilization of Secondary Structure in Soluble Proteins

Bordo, Domenico, Argos, Patrick·1994·Journal of Molecular Biology

DOI 10.1006/jmbi.1994.1676

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Abstract

Intra-molecular side-chain:main-chain (sch:mch) and side-chain (sch:sch) hydrogen bonds observed in 44 well refined crystallographic protein structures with non-homologous sequences have been identified, classified and analysed to detect recurring structural patterns. Each observed bond was characterized by the position of its acceptor and donor groups relative to the N and C termini of the particular secondary structure in which they occur and according to their appearance within the same of sequentially separated secondary structures. The role of short-range hydrogen bonds in the formation and stabilization of a secondary structure and the importance of long-range hydrogen bonds as a cohesive force for different structural segments were also examined. It was found that the N terminus of alpha-helices is characterized by recurring sch:mch and sch:sch bonds with elements of the preceding coil segment, while at the C terminus a frequent intra-helix sch:mch hydrogen bond was frequently observed. The residues at or near the beta-strand termini often cross-linked, through hydrogen-bonding, non-sequential coil segments. Coil structures were characterized by recurring, internal sch:mch hydrogen bonding involving small polar side-chain groups situated at or near their N termini (coil N-capping). The significance of hydrogen bonds as formers and stabilizers of a protein fold and the association of its secondary structural units was also considered through an examination of bond density and distribution throughout the protein tertiary structure.

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Authors: Bordo, D., & Argos, P.
Affiliations: University of Genoa (IT)
European Molecular Biology Laboratory (IT)
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 1994-10
Volume: 243
Issue: 3
Pages: 504-519
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1006/jmbi.1994.1676
OpenAlex: W2086033193
Cited by: 73
References: 0
Citations by year: 2026: 2 · 2025: 5 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 1
FWCI: 1.39
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
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 › Structural Biology › Enzyme Structure and Function
Keywords: protein secondary structure, alpha-helix, beta-strand, coil regions, hydrogen bond density, protein tertiary structure
MeSH terms: Amino Acids, Hydrogen Bonding, Proteins, Molecular Structure, Protein Structure, Secondary, Protein Folding

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The Role of Side-chain Hydrogen Bonds in the Formation and Stabilization of Secondary Structure in Soluble Proteins

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