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Strength of the CαH··O Hydrogen Bond of Amino Acid Residues
Open accessAbstract
Although the peptide C(alpha)H group has historically not been thought to form hydrogen bonds within proteins, ab initio quantum calculations show it to be a potent proton donor. Its binding energy to a water molecule lies in the range between 1.9 and 2.5 kcal/mol for nonpolar and polar amino acids; the hydrogen bond (H-bond) involving the charged lysine residue is even stronger than a conventional OH..O interaction. The preferred H-bond lengths are quite uniform, about 3.32 A. Formation of each interaction results in a downfield shift of the bridging hydrogen's chemical shift and a blue shift in the C(alpha)H stretching frequency, potential diagnostics of the presence of such an H-bond within a protein.
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Cited by
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Sarkhel, S., & Desiraju, G. R. (2004) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10567 · Cited by 285
Metadata
- Authors
- Scheiner, S., Kar, T., & Gu, Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 276
- Issue
- 13
- Pages
- 9832-9837
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1551351981
- Cited by
- 305
- References
- 0
- FWCI
- 15.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Scheiner, S., Kar, T., & Gu, Y. (2001). Strength of the CαH··O Hydrogen Bond of Amino Acid Residues. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m010770200
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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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