Literature DB >> 28495511

Biomolecular NMR: Past and future.

John L Markley1, William Milo Westler2.   

Abstract

The editors of this special volume suggested this topic, presumably because of the perspective lent by our combined >90-year association with biomolecular NMR. What follows is our personal experience with the evolution of the field, which we hope will illustrate the trajectory of change over the years. As for the future, one can confidently predict that it will involve unexpected advances. Our narrative is colored by our experience in using the NMR Facility for Biomedical Studies at Carnegie-Mellon University (Pittsburgh) and in developing similar facilities at Purdue (1977-1984) and the University of Wisconsin-Madison (1984-). We have enjoyed developing NMR technology and making it available to collaborators and users of these facilities. Our group's association with the Biological Magnetic Resonance data Bank (BMRB) and with the Worldwide Protein Data Bank (wwPDB) has also been rewarding. Of course, many groups contributed to the early growth and development of biomolecular NMR, and our brief personal account certainly omits many important milestones.
Copyright © 2017 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Biomolecular NMR history; Computational approaches; NMR instrumentation; Pulse sequence development; Sample preparation and labeling

Mesh:

Year:  2017        PMID: 28495511      PMCID: PMC5701516          DOI: 10.1016/j.abb.2017.05.003

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  95 in total

1.  The charge-relay system of serine proteinases: proton magnetic resonance titration studies of the four histidines of porcine trypsin.

Authors:  J L Markley; M A Porubcan
Journal:  J Mol Biol       Date:  1976-04-15       Impact factor: 5.469

2.  Proton magnetic resonance investigation of enzyme-coenzyme complexes.

Authors:  O JARDETZKY; N G WADE; J J FISCHER
Journal:  Nature       Date:  1963-01-12       Impact factor: 49.962

3.  (19)F-modified proteins and (19)F-containing ligands as tools in solution NMR studies of protein interactions.

Authors:  Naima G Sharaf; Angela M Gronenborn
Journal:  Methods Enzymol       Date:  2015-06-16       Impact factor: 1.600

4.  Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motion.

Authors:  J Fejzo; A M Krezel; W M Westler; S Macura; J L Markley
Journal:  Biochemistry       Date:  1991-04-23       Impact factor: 3.162

5.  High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.

Authors:  G Robillard; R G Shulman
Journal:  J Mol Biol       Date:  1974-07-05       Impact factor: 5.469

6.  NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

Authors:  F Delaglio; S Grzesiek; G W Vuister; G Zhu; J Pfeifer; A Bax
Journal:  J Biomol NMR       Date:  1995-11       Impact factor: 2.835

7.  Crystal structure analysis and refinement of two variants of trigonal trypsinogen: trigonal trypsin and PEG (polyethylene glycol) trypsinogen and their comparison with orthorhombic trypsin and trigonal trypsinogen.

Authors:  W Bode; R Huber
Journal:  FEBS Lett       Date:  1978-06-15       Impact factor: 4.124

8.  Hyperfine-shifted 13C resonance assignments in an iron-sulfur protein with quantum chemical verification: aliphatic C-H···S 3-center-4-electron interactions.

Authors:  William M Westler; I-Jin Lin; András Perczel; Frank Weinhold; John L Markley
Journal:  J Am Chem Soc       Date:  2011-01-05       Impact factor: 15.419

9.  In support of the BMRB.

Authors:  John L Markley; Hideo Akutsu; Tetsuo Asakura; Marc Baldus; Rolf Boelens; Alexandre Bonvin; Robert Kaptein; Ad Bax; Irina Bezsonova; Michael R Gryk; Jeffrey C Hoch; Dmitry M Korzhnev; Mark W Maciejewski; Dave Case; Walter J Chazin; Timothy A Cross; Sonja Dames; Horst Kessler; Oliver Lange; Tobias Madl; Bernd Reif; Michael Sattler; David Eliezer; Alan Fersht; Julie Forman-Kay; Lewis E Kay; James Fraser; John Gross; Tanja Kortemme; Andrej Sali; Toshimichi Fujiwara; Kevin Gardner; Xuelian Luo; Jose Rizo-Rey; Michael Rosen; Roberto R Gil; Chien Ho; Gordon Rule; Angela M Gronenborn; Rieko Ishima; Judith Klein-Seetharaman; Pei Tang; Patrick van der Wel; Yan Xu; Stephan Grzesiek; Sebastian Hiller; Joachim Seelig; Ernest D Laue; Helen Mott; Daniel Nietlispach; Igor Barsukov; Lu-Yun Lian; David Middleton; Tharin Blumenschein; Geoffrey Moore; Iain Campbell; Jason Schnell; Ioannis John Vakonakis; Anthony Watts; Maria R Conte; James Mason; Mark Pfuhl; Mark R Sanderson; Jeremy Craven; Michael Williamson; Cyril Dominguez; Gordon Roberts; Ulrich Günther; Michael Overduin; Joern Werner; Philip Williamson; Claudia Blindauer; Matthew Crump; Paul Driscoll; Tom Frenkiel; Alexander Golovanov; Steve Matthews; John Parkinson; Dusan Uhrin; Mark Williams; David Neuhaus; Hartmut Oschkinat; Andres Ramos; David E Shaw; Christoph Steinbeck; Michele Vendruscolo; Geerten W Vuister; Kylie J Walters; Harel Weinstein; Kurt Wüthrich; Shigeyuki Yokoyama
Journal:  Nat Struct Mol Biol       Date:  2012-09       Impact factor: 15.369

10.  The Complex Energy Landscape of the Protein IscU.

Authors:  Jameson R Bothe; Marco Tonelli; Ibrahim K Ali; Ziqi Dai; Ronnie O Frederick; William M Westler; John L Markley
Journal:  Biophys J       Date:  2015-09-01       Impact factor: 4.033

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