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NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes

NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes
Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity. They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/- 0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.
compatible solute, rubredoxin, protein stabilization, amide proton exchange, nmrpancreatic trypsin-inhibitor, amide proton-exchange, naturally-occurring osmolytes, pyrococcus-furiosus, hydrogen-exchange, glutamate-dehydrogenase, thermococcus-litoralis, globular-proteins, thermal-stability, 2-dimensional nmr
1431-0651
303-311
Lamosa, Pedro
9c2fdf0a-8bc3-4ed6-b295-f26bc448bfd7
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Vis, Hans
756dd51b-fc2a-4bc0-9566-a002c2489990
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Santos, Helena
1c7cb520-ed15-41e7-b381-467ca075ed30
Lamosa, Pedro
9c2fdf0a-8bc3-4ed6-b295-f26bc448bfd7
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Vis, Hans
756dd51b-fc2a-4bc0-9566-a002c2489990
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Santos, Helena
1c7cb520-ed15-41e7-b381-467ca075ed30

Lamosa, Pedro, Brennan, Lorraine, Vis, Hans, Turner, David L. and Santos, Helena (2001) NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes. Extremophiles, 5 (5), 303-311. (doi:10.1007/s007920100206).

Record type: Article

Abstract

Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity. They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/- 0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.

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More information

Published date: 1 October 2001
Keywords: compatible solute, rubredoxin, protein stabilization, amide proton exchange, nmrpancreatic trypsin-inhibitor, amide proton-exchange, naturally-occurring osmolytes, pyrococcus-furiosus, hydrogen-exchange, glutamate-dehydrogenase, thermococcus-litoralis, globular-proteins, thermal-stability, 2-dimensional nmr

Identifiers

Local EPrints ID: 19536
URI: http://eprints.soton.ac.uk/id/eprint/19536
ISSN: 1431-0651
PURE UUID: 87b8543d-3f79-4fdc-b738-6247f1c46f74

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Date deposited: 15 Feb 2006
Last modified: 15 Jul 2019 19:27

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Contributors

Author: Pedro Lamosa
Author: Lorraine Brennan
Author: Hans Vis
Author: David L. Turner
Author: Helena Santos

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