{"title":"氢键生物系统研究中同位素对化学位移的影响","authors":"Poul Erik Hansen","doi":"10.1016/j.pnmrs.2020.08.001","DOIUrl":null,"url":null,"abstract":"<div><p>This review deals with biological systems and with deuterium isotope effects on chemical shifts caused by the replacement of OH, NH or SH protons by deuterons. Hydrogen bonding is clearly of central importance. Isotope effects on chemical shifts seems very suitable for use in studies of structures and reactions in the interior of proteins, as exchange of the label can be expected to be slow. One-bond deuterium isotope effects on <sup>15</sup>N chemical shifts, and two-bond effects on <sup>1</sup>H chemical shifts for N(D)H<sub>x</sub> systems can be used to gauge hydrogen bond strength in proteins as well as in salt bridges. Solvent isotope effects on <sup>19</sup>F chemical shifts show promise in monitoring solvent access. Equilibrium isotope effects need in some cases to be taken into account. Schemes for calculation of deuterium isotope effects on chemical shifts are discussed and it is demonstrated how calculations may be used in the study of complex biological systems.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"120 ","pages":"Pages 109-117"},"PeriodicalIF":7.3000,"publicationDate":"2020-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2020.08.001","citationCount":"4","resultStr":"{\"title\":\"Isotope effects on chemical shifts in the study of hydrogen bonded biological systems\",\"authors\":\"Poul Erik Hansen\",\"doi\":\"10.1016/j.pnmrs.2020.08.001\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>This review deals with biological systems and with deuterium isotope effects on chemical shifts caused by the replacement of OH, NH or SH protons by deuterons. Hydrogen bonding is clearly of central importance. Isotope effects on chemical shifts seems very suitable for use in studies of structures and reactions in the interior of proteins, as exchange of the label can be expected to be slow. One-bond deuterium isotope effects on <sup>15</sup>N chemical shifts, and two-bond effects on <sup>1</sup>H chemical shifts for N(D)H<sub>x</sub> systems can be used to gauge hydrogen bond strength in proteins as well as in salt bridges. Solvent isotope effects on <sup>19</sup>F chemical shifts show promise in monitoring solvent access. Equilibrium isotope effects need in some cases to be taken into account. Schemes for calculation of deuterium isotope effects on chemical shifts are discussed and it is demonstrated how calculations may be used in the study of complex biological systems.</p></div>\",\"PeriodicalId\":20740,\"journal\":{\"name\":\"Progress in Nuclear Magnetic Resonance Spectroscopy\",\"volume\":\"120 \",\"pages\":\"Pages 109-117\"},\"PeriodicalIF\":7.3000,\"publicationDate\":\"2020-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.pnmrs.2020.08.001\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Progress in Nuclear Magnetic Resonance Spectroscopy\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0079656520300248\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Progress in Nuclear Magnetic Resonance Spectroscopy","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0079656520300248","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Isotope effects on chemical shifts in the study of hydrogen bonded biological systems
This review deals with biological systems and with deuterium isotope effects on chemical shifts caused by the replacement of OH, NH or SH protons by deuterons. Hydrogen bonding is clearly of central importance. Isotope effects on chemical shifts seems very suitable for use in studies of structures and reactions in the interior of proteins, as exchange of the label can be expected to be slow. One-bond deuterium isotope effects on 15N chemical shifts, and two-bond effects on 1H chemical shifts for N(D)Hx systems can be used to gauge hydrogen bond strength in proteins as well as in salt bridges. Solvent isotope effects on 19F chemical shifts show promise in monitoring solvent access. Equilibrium isotope effects need in some cases to be taken into account. Schemes for calculation of deuterium isotope effects on chemical shifts are discussed and it is demonstrated how calculations may be used in the study of complex biological systems.
期刊介绍：
Progress in Nuclear Magnetic Resonance Spectroscopy publishes review papers describing research related to the theory and application of NMR spectroscopy. This technique is widely applied in chemistry, physics, biochemistry and materials science, and also in many areas of biology and medicine. The journal publishes review articles covering applications in all of these and in related subjects, as well as in-depth treatments of the fundamental theory of and instrumental developments in NMR spectroscopy.
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