The effect of loops on the structural organization of alpha-helical membrane proteins

scientific article published on March 2009

The effect of loops on the structural organization of alpha-helical membrane proteins is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.BPJ.2008.12.3894
P932PMC publication ID2717299
P698PubMed publication ID19289056
P5875ResearchGate publication ID24203461

P50authorJudith Klein-SeetharamanQ47565784
P2093author name stringHagai Meirovitch
Oznur Tastan
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Bacteriorhodopsin can be refolded from two independently stable transmembrane helixes and the complementary five-helix fragmentQ41127203
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A structural role of the carotenoid in the light-harvesting II protein of Rhodobacter capsulatusQ42796666
GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophilesQ43030311
Structure and function in bacteriorhodopsin: the role of the interhelical loops in the folding and stability of bacteriorhodopsin.Q43591536
Structure and function in bacteriorhodopsin: the effect of the interhelical loops on the protein folding kineticsQ43591539
Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranesQ43733411
P433issue6
P407language of work or nameEnglishQ1860
P921main subjectmembrane proteinQ423042
P304page(s)2299-2312
P577publication date2009-03-01
P1433published inBiophysical JournalQ2032955
P1476titleThe effect of loops on the structural organization of alpha-helical membrane proteins
P478volume96

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cites work (P2860)
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