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Title: Isotope labeling for NMR studies of macromolecular structure and interactions

Abstract

Implementation of biosynthetic methods for uniform or specific isotope labeling of proteins, coupled with the recent development of powerful heteronuclear multidimensional NMR methods, has led to a dramatic increase in the size and complexity of macromolecular systems that are now amenable to NMR structural analysis. In recent years, a new technology has emerged that combines uniform {sup 13}C, {sup 15}N labeling with heteronuclear multidimensional NMR methods to allow NMR structural studies of systems approaching 25 to 30 kDa in molecular weight. In addition, with the introduction of specific {sup 13}C and {sup 15}N labels into ligands, meaningful NMR studies of complexes of even higher molecular weight have become feasible. These advances usher in a new era in which the earlier, rather stringent molecular weight limitations have been greatly surpassed and NMR can begin to address many central biological problems that involve macromolecular structure, dynamics, and interactions.

Authors:
 [1]
  1. Scripps Research Institute, La Jolla, CA (United States)
Publication Date:
Research Org.:
Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
OSTI Identifier:
83371
Report Number(s):
LA-12893-C; CONF-9403228-
ON: DE95012795; CNN: Grant GM36643;Grant CA27498; TRN: 95:004732-0001
Resource Type:
Conference
Resource Relation:
Conference: Stable isotope applications in biomolecular structure and mechanisms, Santa Fe, NM (United States), 27-31 Mar 1994; Other Information: PBD: Dec 1994; Related Information: Is Part Of Stable isotope applications in biomolecular structure and mechanisms. A meeting to bring together producers and users of stable-isotope-labeled compounds to assess current and future needs; Trewhella, J.; Cross, T.A.; Unkefer, C.J. [eds.]; PB: 382 p.
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; 40 CHEMISTRY; PROTEINS; NMR IMAGING; MOLECULAR STRUCTURE; STRUCTURAL CHEMICAL ANALYSIS; ISOTOPE APPLICATIONS; LIGANDS; MOLECULAR WEIGHT; LABELLING; CARBON 13; NITROGEN 15

Citation Formats

Wright, P E. Isotope labeling for NMR studies of macromolecular structure and interactions. United States: N. p., 1994. Web.
Wright, P E. Isotope labeling for NMR studies of macromolecular structure and interactions. United States.
Wright, P E. 1994. "Isotope labeling for NMR studies of macromolecular structure and interactions". United States. https://www.osti.gov/servlets/purl/83371.
@article{osti_83371,
title = {Isotope labeling for NMR studies of macromolecular structure and interactions},
author = {Wright, P E},
abstractNote = {Implementation of biosynthetic methods for uniform or specific isotope labeling of proteins, coupled with the recent development of powerful heteronuclear multidimensional NMR methods, has led to a dramatic increase in the size and complexity of macromolecular systems that are now amenable to NMR structural analysis. In recent years, a new technology has emerged that combines uniform {sup 13}C, {sup 15}N labeling with heteronuclear multidimensional NMR methods to allow NMR structural studies of systems approaching 25 to 30 kDa in molecular weight. In addition, with the introduction of specific {sup 13}C and {sup 15}N labels into ligands, meaningful NMR studies of complexes of even higher molecular weight have become feasible. These advances usher in a new era in which the earlier, rather stringent molecular weight limitations have been greatly surpassed and NMR can begin to address many central biological problems that involve macromolecular structure, dynamics, and interactions.},
doi = {},
url = {https://www.osti.gov/biblio/83371}, journal = {},
number = ,
volume = ,
place = {United States},
year = {Thu Dec 01 00:00:00 EST 1994},
month = {Thu Dec 01 00:00:00 EST 1994}
}

Conference:
Other availability
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