{"title":"Chapter 22.3 Hydrogen bonding in biological macromolecules","authors":"E. Baker","doi":"10.1107/97809553602060000887","DOIUrl":null,"url":null,"abstract":"Hydrogen bonds are weak non-covalent interactions, but their directional nature and the large number of hydrogen-bonding groups mean that they play a critical role in the structure and function of proteins and nucleic acids. Analyses of three-dimensional structures, particularly of proteins, reveal many consistent patterns, which are described in this review. Protein structures show almost complete saturation of hydrogen-bonding potential. Helices, β-strands, β-turns and γ-turns all show characteristic C=O···HN geometries, with helices having a variety of termination patterns. Local interactions are very common for main-chain···side-chain hydrogen bonds and may help direct protein folding. Non-local interactions, although fewer in number, can be very important for structural stability, and bound water molecules, because of their double-donor, double-acceptor capability, can play critical roles in satisfying overall hydrogen-bonding requirements. Finally, there is also a growing realization that non-conventional hydrogen bonds may play a more important role than hitherto recognized. \n \n \nKeywords: \n \nbeta-sheets; \namino-aromatic hydrogen bonding; \nDNA; \nhelices; \nhydrogen bonding; \nhydrogen-bonding criteria; \nhydrogen-bonding potential; \nnucleic acids; \nprotein folding; \nprotein stability; \nRNA; \nsecondary structure; \nside-chain hydrogen bonding; \nturns","PeriodicalId":338076,"journal":{"name":"International Tables for Crystallography","volume":"68 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2012-04-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Tables for Crystallography","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1107/97809553602060000887","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Hydrogen bonds are weak non-covalent interactions, but their directional nature and the large number of hydrogen-bonding groups mean that they play a critical role in the structure and function of proteins and nucleic acids. Analyses of three-dimensional structures, particularly of proteins, reveal many consistent patterns, which are described in this review. Protein structures show almost complete saturation of hydrogen-bonding potential. Helices, β-strands, β-turns and γ-turns all show characteristic C=O···HN geometries, with helices having a variety of termination patterns. Local interactions are very common for main-chain···side-chain hydrogen bonds and may help direct protein folding. Non-local interactions, although fewer in number, can be very important for structural stability, and bound water molecules, because of their double-donor, double-acceptor capability, can play critical roles in satisfying overall hydrogen-bonding requirements. Finally, there is also a growing realization that non-conventional hydrogen bonds may play a more important role than hitherto recognized.
Keywords:
beta-sheets;
amino-aromatic hydrogen bonding;
DNA;
helices;
hydrogen bonding;
hydrogen-bonding criteria;
hydrogen-bonding potential;
nucleic acids;
protein folding;
protein stability;
RNA;
secondary structure;
side-chain hydrogen bonding;
turns