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Adaptation of low-resolution methods for the study of yeast microsomal polytopic membrane proteins: a methodological review.
MedLine Citation:
PMID:  23356255     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Most integral membrane proteins of yeast with two or more membrane-spanning sequences have not yet been crystallized and for many of them the side on which the active sites or ligand-binding domains reside is unknown. Also, bioinformatic topology predictions are not yet fully reliable. However, so-called low-resolution biochemical methods can be used to locate hydrophilic loops or individual residues of polytopic membrane proteins at one or the other side of the membrane. The advantages and limitations of several such methods for topological studies with yeast ER integral membrane proteins are discussed. We also describe new tools that allow us to better control and validate results obtained with SCAM (substituted cysteine accessibility method), an approach that determines the position of individual residues with respect to the membrane plane, whereby only minimal changes in the primary sequence have to be introduced into the protein of interest.
Authors:
Arlette Bochud; Nagaraju Ramachandra; Andreas Conzelmann
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemical Society transactions     Volume:  41     ISSN:  1470-8752     ISO Abbreviation:  Biochem. Soc. Trans.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7506897     Medline TA:  Biochem Soc Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  35-42     Citation Subset:  IM    
Affiliation:
*Department of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland.
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