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NMR‐profiles of protein solutions
Author(s) -
Pedrini Bill,
Serrano Pedro,
Mohanty Biswaranjan,
Geralt Michael,
Wüthrich Kurt
Publication year - 2013
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22348
Subject(s) - chemistry , microscale chemistry , sequence (biology) , structural genomics , resonance (particle physics) , nuclear magnetic resonance spectroscopy , two dimensional nuclear magnetic resonance spectroscopy , nmr spectra database , protein structure , nuclear magnetic resonance , analytical chemistry (journal) , spectral line , stereochemistry , biochemistry , chromatography , physics , mathematics education , astronomy , mathematics , particle physics
NMR‐Profiles are quantitative one‐dimensional (1D) presentations of 2D [ 15 N, 1 H]‐correlation spectra used to monitor the quality of protein solutions prior to and during NMR structure determinations and functional studies. In our current use in structural genomics projects, an NMR‐Profile is recorded at the outset of a structure determination, using a uniformly 15 N‐labeled microscale sample of the protein. We thus assess the extent to which polypeptide backbone resonance assignments can be achieved with given NMR techniques, for example, conventional triple resonance experiments or APSY‐NMR. With the availability of sequence‐specific polypeptide backbone resonance assignments in the course of the structure determination, an “Assigned NMR‐Profile” is generated, which visualizes the variation of the 15 N– 1 H correlation cross peak intensities along the sequence and thus maps the sequence locations of polypeptide segments for which the NMR line shapes are affected by conformational exchange or other processes. The Assigned NMR‐Profile provides a guiding reference during later stages of the structure determination, and is of special interest for monitoring the protein during functional studies, where dynamic features may be modulated during physiological processes. © 2013 Wiley Periodicals, Inc. Biopolymers 99: 825–831, 2013.