Document Detail


1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.
MedLine Citation:
PMID:  1483454     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1H-NMR assignments have been defined for the aromatic-ring protons of the bovine, guinea pig and human variants of alpha-lactalbumin. Spin-system networks were identified by means of double-quantum-filtered two-dimensional J-correlated spectroscopy and two-dimensional relayed coherence spectroscopy data. Analysis of two-dimensional nuclear-Overhauser-enhancement spectroscopy data of the proteins indicated that in each case two clusters of aromatic residues exist. The two clusters are also evident in the crystal structure of the human protein, and this evidence, in conjunction with sequence differences between the three proteins, permitted sequence-specific assignments to be made for the majority of aromatic residues. Remaining ambiguities in the assignments could be resolved by analysis of photochemically induced dynamic nuclear polarization (PCIDNP) effects. Comparison of the PCIDNP spectra of the three proteins indicated the presence of only minor differences in the surface exposure of conserved aromatic residues. Taken together, these results indicate that the environments of the conserved aromatic residues in bovine, guinea pig and human alpha-lactalbumin in solution are very similar to each other, and that the solution and the crystal forms of at least the human protein are similar.
Authors:
A T Alexandrescu; R W Broadhurst; C Wormald; C L Chyan; J Baum; C M Dobson
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  210     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1992 Dec 
Date Detail:
Created Date:  1993-02-18     Completed Date:  1993-02-18     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  699-709     Citation Subset:  IM    
Affiliation:
Inorganic Chemistry Laboratory, Oxford University, England.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cattle
Genetic Variation
Guinea Pigs
Histidine*
Humans
Hydrogen
Lactalbumin / chemistry*
Magnetic Resonance Spectroscopy / methods
Muramidase / chemistry
Protein Conformation*
Grant Support
ID/Acronym/Agency:
GM-45302/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
1333-74-0/Hydrogen; 71-00-1/Histidine; 9013-90-5/Lactalbumin; EC 3.2.1.17/Muramidase

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


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