Document Detail


Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).
MedLine Citation:
PMID:  20572250     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The sequence-specific resonance assignment of a protein forms the basis for studies of molecular structure and dynamics, as well as to functional assay studies by NMR spectroscopy. Here we present a protocol for the sequential 13C and 15N resonance assignment of uniformly [15N,13C]-labeled proteins, based on a suite of complementary three-dimensional solid-state NMR spectroscopy experiments. It is directed towards the application to proteins with more than about 100 amino acid residues. The assignments rely on a walk along the backbone by using a combination of three experiments that correlate nitrogen and carbon spins, including the well-dispersed Cbeta resonances. Supplementary spectra that correlate further side-chain resonances can be important for identifying the amino acid type, and greatly assist the assignment process. We demonstrate the application of this assignment protocol for a crystalline preparation of the N-terminal globular domain of the HET-s prion, a 227-residue protein.
Authors:
Anne Schuetz; Christian Wasmer; Birgit Habenstein; René Verel; Jason Greenwald; Roland Riek; Anja Böckmann; Beat H Meier
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chembiochem : a European journal of chemical biology     Volume:  11     ISSN:  1439-7633     ISO Abbreviation:  Chembiochem     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-26     Completed Date:  2010-11-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100937360     Medline TA:  Chembiochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  1543-51     Citation Subset:  IM    
Affiliation:
Physical Chemistry, ETH Zürich, 8093 Zürich, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Carbon Isotopes
Magnetic Resonance Spectroscopy / methods*
Nitrogen Isotopes
Prions / chemistry
Proteins / chemistry*
Research Design
Chemical
Reg. No./Substance:
0/Carbon Isotopes; 0/Nitrogen Isotopes; 0/Prions; 0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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