Jump to ContentJump to Main Navigation
Biological NMR Spectroscopy$
Users without a subscription are not able to see the full content.

John L. Markley and Stanley J. Opella

Print publication date: 1997

Print ISBN-13: 9780195094688

Published to Oxford Scholarship Online: November 2020

DOI: 10.1093/oso/9780195094688.001.0001

Show Summary Details
Page of

PRINTED FROM OXFORD SCHOLARSHIP ONLINE (oxford.universitypressscholarship.com). (c) Copyright Oxford University Press, 2021. All Rights Reserved. An individual user may print out a PDF of a single chapter of a monograph in OSO for personal use. date: 23 October 2021

NMR of Larger Proteins: Approach to the Structural Analyses of Antibody

NMR of Larger Proteins: Approach to the Structural Analyses of Antibody

Chapter:
(p.183) 14 NMR of Larger Proteins: Approach to the Structural Analyses of Antibody
Source:
Biological NMR Spectroscopy
Author(s):

Yoji Arata

Publisher:
Oxford University Press
DOI:10.1093/oso/9780195094688.003.0020

The first 1H NMR spectrum of a protein, bovine pancreatic ribonuclease, reported in 1957 by Saunders et al. was accounted for by Jardetzky and Jardetzky (1957) in terms of the spectra of the constituent ammo acids. Jardetzky and coworkers continued to report a series of important papers describing the potential usefulness of high-resolution NMR (Roberts and Jardetzky, 1970). Modern NMR of proteins began with the classic paper published in 1968 by Markley, Putter, and Jardetzky, who beautifully demonstrated the possibility of using stable-isotope labeling for the structural analyses of proteins in solution (Markley et al., 1968). Five years before the publication of this paper, Jardetzky gave an important lecture in Tokyo, stressing the importance of NMR particularly in combination with deuterium labeling as a potential solution version of X-ray crystallography for the determination of the three-dimensional structure of proteins (Jardetzky, 1965). The impact of Jardetzky’s contribution was great, eventually leading to the now well-established combination of multidimensional NMR and stable-isotope labeling for the determination of the three-dimensional structure of proteins in solution. High-resolution NMR of biological macromolecules takes advantage of the fact that 1H, 13C, and 15N, all of which are spin 1/2 nuclei, possess long relaxation times, which primarily are due to weak dipole-dipole interactions. Thus, phase memory can be retained long enough to extract relevant information on the spin system by fully making use of multidimensional techniques. This makes high-resolution NMR special as a tool for structural analyses at atomic resolution. By contrast, relaxation times are far shorter in the case of visible, ultraviolet, infrared, and Raman spectroscopy, where much stronger interactions are involved. For this reason no structural analyses at atomic resolution are possible using these types of spectroscopy. However, an increase in the molecular weight eventually creates difficulties in achieving sufficient spectral resolution to be able to separate and assign each of the resonances of a protein. This is due to 1) a limitation of the strength of static magnetic field available and more importantly 2) an unavoidable shortening of relaxation times originating from the slow tumbling motion of the protein molecules in solution.

Keywords:   antigen, immunoglobulin, paramagnetic ions

Oxford Scholarship Online requires a subscription or purchase to access the full text of books within the service. Public users can however freely search the site and view the abstracts and keywords for each book and chapter.

Please, subscribe or login to access full text content.

If you think you should have access to this title, please contact your librarian.

To troubleshoot, please check our FAQs , and if you can't find the answer there, please contact us .