Sequence specific ¹H, ¹³C and ¹⁵N resonance assignments of hahellin in 8 M urea

The sequence specific ¹H, ¹³C and ¹⁵N resonance assignments of hahellin in 8 M urea-denatured state have been accomplished by NMR spectroscopy. Secondary chemical shift analysis reveals the native-like propensities for β-rich conformation in the denatured state.

Saved in:
Bibliographic Details
Published inBiomolecular NMR assignments Vol. 4; no. 2; pp. 163 - 165
Main Authors Srivastava, Atul K, Chary, K. V. R
Format Journal Article
LanguageEnglish
Published Dordrecht Dordrecht : Springer Netherlands 01.10.2010
Springer Netherlands
Springer Nature B.V
Subjects
Amino Acid Sequence
Biochemistry
Biological and Medical Physics
Biophysics
Carbon Isotopes
Crystallins - chemistry
Gammaproteobacteria - chemistry
Greek key
Hahellin
Hydrogen
Nitrogen Isotopes
NMR
NMR resonance assignment
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Denaturation - drug effects
Protein folding
Protein Structure, Secondary
Spectrum analysis
Urea - pharmacology
βγ-Crystallin
Hahellin
Greek key
Protein folding
βγ-Crystallin
NMR resonance assignment
Online AccessGet full text

Cover

More Information
Summary:The sequence specific ¹H, ¹³C and ¹⁵N resonance assignments of hahellin in 8 M urea-denatured state have been accomplished by NMR spectroscopy. Secondary chemical shift analysis reveals the native-like propensities for β-rich conformation in the denatured state.
Bibliography:http://dx.doi.org/10.1007/s12104-010-9234-9
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-010-9234-9