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

AUTOR(ES)

Wand, A. Joshua

FONTE

The National Academy of Sciences

RESUMO

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.

Documentos Relacionados

• High-resolution solid-state NMR of quadrupolar nuclei
• Behavioral analysis of Vibrio parahaemolyticus variants in high- and low-viscosity microenvironments by use of digital image processing.
• High-resolution computed tomography.
• High-Resolution Shadowing of Transfer RNA
• High-resolution simulations of gravity currents