Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: How well can we do

被引：0

作者：

Hansen, D. Flemming ^{[1
]}

Vallurupalli, Pramodh ^{[1
]}

Lundström, Patrik ^{[1
]}

Neudecker, Philipp ^{[1
]}

Kay, Lewis E. ^{[1
]}

机构：

[1] Departments of Medical Genetics, Biochemisty and Chemistry, University of Toronto, Toronto, ON M5S 1A8, Canada

来源：

Journal of the American Chemical Society | 1600年 / 130卷 / 08期

关键词：

Carr-Purcell-Meiboom-Gill relaxation dispersion NMR spectroscopy has evolved into a powerful approach for the study of low populated; invisible conformations of biological molecules. One of the powerful features of the experiment is that chemical shift differences between the exchanging conformers can be obtained; providing structural information about invisible excited states. Through the development of new labeling approaches and NMR experiments it is now possible to measure backbone 13Cα and 13CO relaxation dispersion profiles in proteins without complications from 13C-13C couplings. Such measurements are presented here; along with those that probe exchange using 15N and 1HN nuclei. A key experimental design has been the choice of an exchanging system where excited-state chemical shifts were known from independent measurement. Thus it is possible to evaluate quantitatively the accuracy of chemical shift differences obtained in dispersion experiments and to establish that in general very accurate values can be obtained. The experimental work is supplemented by computations that suggest that similarly accurate shifts can be measured in many cases for systems with exchange rates and populations that fall within the range of those that can be quantified by relaxation dispersion. The accuracy of the extracted chemical shifts opens up the possibility of obtaining quantitative structural information of invisible states of the sort that is now available from chemical shifts recorded on ground states of proteins. © 2008 American Chemical Society;

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摘要：

Journal article (JA)

引用

页码：2667 / 2675

共 27 条

[1] Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy:: How well can we do?
Hansen, D. Flemming
Vallurupalli, Pramodh
Lundstrom, Patrik
Neudecker, Philipp
Kay, Lewis E.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (08) : 2667 - 2675
[2] Measuring 13Cβ chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy
Patrik Lundström
Hong Lin
Lewis E. Kay
Journal of Biomolecular NMR, 2009, 44 : 139 - 155
[3] Measuring 13Cβ chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy
Lundstrom, Patrik
Lin, Hong
Kay, Lewis E.
JOURNAL OF BIOMOLECULAR NMR, 2009, 44 (03) : 139 - 155
[4] Probing structure in invisible protein states with anisotropic NMR chemical shifts
Vallurupalli, Pramodh
Hansen, D. Flemming
Kay, Lewis E.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (09) : 2734 - +
[5] Probing structure in invisible protein states with anisotropic NMR chemical shifts
Vallurupalli, Pramodh
Hansen, D. Flemming
Kay, Lewis E.
Journal of the American Chemical Society, 2008, 130 (09): : 2734 - 2735
[6] Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy
Baldwin, Andrew J.
Hansen, D. Flemming
Vallurupalli, Pramodh
Kay, Lewis E.
Journal of the American Chemical Society, 2009, 131 (33): : 11939 - 11948
[7] Measurement of Methyl Axis Orientations in Invisible, Excited States of Proteins by Relaxation Dispersion NMR Spectroscopy
Baldwin, Andrew J.
Hansen, D. Flemming
Vallurupalli, Pramodh
Kay, Lewis E.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2009, 131 (33) : 11939 - 11948
[8] Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
Vallurupalli, Pramodh
Hansen, D. Flemming
Kay, Lewis E.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (33) : 11766 - 11771
[9] Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding
Korzhnev, Dmitry M.
Kay, Lewis E.
ACCOUNTS OF CHEMICAL RESEARCH, 2008, 41 (03) : 442 - 451
[10] Accurate Measurement of Alpha Proton Chemical Shifts of Excited Protein States by Relaxation Dispersion NMR Spectroscopy
Lundstroem, Patrik
Hansen, D. Flemming
Vallurupalli, Pramodh
Kay, Lewis E.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2009, 131 (05) : 1915 - 1926

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