Abstract
Intramolecular hydrogen bonds between different components of molecules stabilize conformation. They are among the most important interactions in small and in large biological molecules because they require particular molecular conformations to be formed, and when formed, they confer additional rotational stability to these conformations. They ultimately help to determine and to define the three-dimensional structures of the molecules, and are therefore involved in their functional aspects. These bonds are of major importance in the globular proteins, where all the secondary and tertiary structure hydrogen bonds are of this type. In polypeptides, the NH· · ·O=C bonds between peptide bonds (n) and (n+3) give rise to β-turns and to 310 helices, and between bonds (n) and (n+4) to α-helices (see Part III, Chapt. 19).
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© 1994 Springer-Verlag Berlin Heidelberg
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Jeffrey, G.A., Saenger, W. (1994). Intramolecular Hydrogen Bonds. In: Hydrogen Bonding in Biological Structures. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-85135-3_9
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DOI: https://doi.org/10.1007/978-3-642-85135-3_9
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-57903-8
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