Document Detail

Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles.
MedLine Citation:
PMID:  6291595     Owner:  NLM     Status:  MEDLINE    
The mitochondrial H+-ATPase proteolipid from Neurospora crassa was incorporated into small unilamellar dimyristoylphosphatidylcholine vesicles and its conformation determined by circular dichroism spectroscopy (CD). While the largely alpha-helical conformation is relatively independent of the method of incorporation into vesicles, i.e., rehydration, detergent dialysis, or detergent dilution, the proteolipid conformation was significantly different in detergent micelles and in organic solvents. Only very slight changes in the CD spectrum were observed upon binding of the H+-ATPase inhibitor dicyclohexylcarbodiimide to the proteolipid in vesicles, thus suggesting that the inhibitor acts either by blocking the channel or by masking an essential charge group, rather by than causing an overall conformational change in the channel. Additionally, very similar CD spectra were obtained for vesicles with different lipid/protein mole ratios, indicating either that no substantial conformational differences exist between monomer and multimers or that monomers self-associate to form stable complexes during incorporation into vesicles. This study has provided a physical basis for model-building studies of the proteolipid channel structure.
D Mao; E Wachter; B A Wallace
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  21     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1982 Sep 
Date Detail:
Created Date:  1983-01-07     Completed Date:  1983-01-07     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4960-8     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphatases*
Circular Dichroism
Ion Channels
Macromolecular Substances
Models, Chemical
Neurospora crassa / cytology
Protein Conformation
Proton-Translocating ATPases
Grant Support
Reg. No./Substance:
0/Ion Channels; 0/Liposomes; 0/Macromolecular Substances; 0/Phosphatidylcholines; 0/Proteolipids; 13699-48-4/Dimyristoylphosphatidylcholine; EC 3.6.1.-/Adenosine Triphosphatases; EC ATPases

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

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