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High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.

PubMed
Authors: Wand AJ, Ehrhardt MR, Flynn PF

Year

1998

Paper ID

13431

Status

Peer-reviewed

Abstract Read

~2 min

Abstract Words

90

Citations

122

Abstract

The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR techniques. The encapsulation of a protein in a reverse micelle dissolved in a low-viscosity fluid allows it to tumble as fast as a much smaller protein. The approach is demonstrated and validated with the protein ubiquitin encapsulated in reverse micelles prepared in a variety of alkane solvents.

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  • This paper contributes to the Quantum Chemistry research area in the Quantum Articles archive.
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  • The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution.

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