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Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy

✍ Scribed by Angela M. Gronenborn; G. Marius Clore


Publisher
Cold Spring Harbor Laboratory Press
Year
2008
Tongue
English
Weight
428 KB
Volume
5
Category
Article
ISSN
0961-8368

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Rapid screening for structural integrity
✍ Angela M. Gronenborn; G. Marius Clore πŸ“‚ Article πŸ“… 2008 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 284 KB

A simple and rapid method based on 15N labeling and 1H-15N heteronuclear single quantum coherence spectroscopy is presented to directly assess the structural integrity of overexpressed proteins in crude Escherichia coli extracts without the need for any purification. The method is demonstrated using

Structural and dynamic characterization
✍ M. Kirsten Frank; G. Marius Clore; Angela M. Gronenborn πŸ“‚ Article πŸ“… 1995 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 1009 KB

## Abstract The structure and dynamics of the urea‐denatured B1 immunoglobulin binding domain of streptococcal protein G (GB1) has been investigated by multidimensional heteronuclear NMR spectroscopy. Complete ^1^H, ^15^N, and ^13^C assignments are obtained by means of sequential through‐bond corre