Peptide Models of Helical Hydrophobic Transmembrane Segments of Membrane Proteins. 2. Differential Scanning Calorimetric and FTIR Spectroscopic Studies of the Interaction of Ac-K2-(LA)12-K2-amide with Phosphatidylcholine Bilayers

Biochemistry ◽  
1995 ◽  
Vol 34 (7) ◽  
pp. 2362-2371 ◽  
Author(s):  
Yuan-Peng Zhang ◽  
Ruthven N. A. H. Lewis ◽  
Robert S. Hodges ◽  
Ronald N. McElhaney
Keyword(s):  
Membrane Proteins ◽  
Spectroscopic Studies ◽  
Differential Scanning Calorimetric ◽  
Transmembrane Segments ◽  
Peptide Models

Peptide Models of the Helical Hydrophobic Transmembrane Segments of Membrane Proteins:  Interactions of Acetyl-K2-(LA)12-K2-Amide with Phosphatidylethanolamine Bilayer Membranes†

Biochemistry ◽  
2001 ◽  
Vol 40 (2) ◽  
pp. 474-482 ◽  
Author(s):  
Yuan-Peng Zhang ◽  
Ruthven N. A. H. Lewis ◽  
Robert S. Hodges ◽  
Ronald N. McElhaney
Keyword(s):  
Membrane Proteins ◽  
Bilayer Membranes ◽  
Transmembrane Segments ◽  
Peptide Models ◽  
Proteins Interactions

Peptide Models of Helical Hydrophobic Transmembrane Segments of Membrane Proteins. 1. Studies of the Conformation, Intrabilayer Orientation, and Amide Hydrogen Exchangeability of Ac-K2-(LA)12-K2-Amide

Biochemistry ◽  
1995 ◽  
Vol 34 (7) ◽  
pp. 2348-2361 ◽  
Author(s):  
Yuan-Peng Zhang ◽  
Ruthven N. A. H. Lewis ◽  
Gillian D. Henry ◽  
Brian D. Sykes ◽  
Robert S. Hodges ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Amide Hydrogen ◽  
Transmembrane Segments ◽  
Peptide Models

Interaction of a peptide model of a hydrophobic transmembrane .alpha.-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies

Biochemistry ◽  
1992 ◽  
Vol 31 (46) ◽  
pp. 11579-11588 ◽  
Author(s):  
Yuan Peng Zhang ◽  
Ruthven N. A. H. Lewis ◽  
Robert S. Hodges ◽  
Ronald N. McElhaney
Keyword(s):  
Membrane Protein ◽  
Spectroscopic Studies ◽  
Differential Scanning Calorimetric ◽  
Helical Segment

The electroneutral cation-chloride cotransporters.

1998 ◽  
Vol 201 (14) ◽  
pp. 2091-2102 ◽  
Author(s):  
D B Mount ◽  
E Delpire ◽  
G Gamba ◽  
A E Hall ◽  
E Poch ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Gene Family ◽  
Molecular Identification ◽  
Membrane Topology ◽  
Cytoplasmic Domains ◽  
Transmembrane Segments ◽  
Novel Gene ◽  
Lower Eukaryotes ◽  
Homologous Genes ◽  
Cation Chloride Cotransporters

Electroneutral cation-chloride cotransporters are widely expressed and perform a variety of physiological roles. A novel gene family of five members, encompassing a Na+-Cl- transporter, two Na+-K+-2Cl- transporters and two K+-Cl- cotransporters, encodes these membrane proteins; homologous genes have also been identified in a prokaryote and a number of lower eukaryotes. The cotransporter proteins share a common predicted membrane topology, with twelve putative transmembrane segments flanked by long hydrophilic N- and C-terminal cytoplasmic domains. The molecular identification of these transporters has had a significant impact on the study of their function, regulation and pathophysiology.

scholarly journals Role of positively charged transmembrane segments in the insertion and assembly of mitochondrial inner-membrane proteins

2001 ◽  
Vol 98 (24) ◽  
pp. 13814-13819 ◽  
Author(s):  
Y. Saint-Georges ◽  
P. Hamel ◽  
C. Lemaire ◽  
G. Dujardin
Keyword(s):  
Membrane Proteins ◽  
Inner Membrane ◽  
Transmembrane Segments ◽  
Mitochondrial Inner Membrane ◽  
Positively Charged

scholarly journals Stability and flexibility of marginally hydrophobic–segment stalling at the endoplasmic reticulum translocon

2016 ◽  
Vol 27 (6) ◽  
pp. 930-940 ◽  
Author(s):  
Yuichiro Kida ◽  
Yudai Ishihara ◽  
Hidenobu Fujita ◽  
Yukiko Onishi ◽  
Masao Sakaguchi
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Lipid Phase ◽  
Endoplasmic Reticulum Membrane ◽  
Dependent Manner ◽  
Transmembrane Segment ◽  
Conducting Channel ◽  
Transmembrane Segments ◽  
Lipid Environment ◽  
Sec61 Channel

Many membrane proteins are integrated into the endoplasmic reticulum membrane through the protein-conducting channel, the translocon. Transmembrane segments with insufficient hydrophobicity for membrane integration are frequently found in multispanning membrane proteins, and such marginally hydrophobic (mH) segments should be accommodated, at least transiently, at the membrane. Here we investigated how mH-segments stall at the membrane and their stability. Our findings show that mH-segments can be retained at the membrane without moving into the lipid phase and that such segments flank Sec61α, the core channel of the translocon, in the translational intermediate state. The mH-segments are gradually transferred from the Sec61 channel to the lipid environment in a hydrophobicity-dependent manner, and this lateral movement may be affected by the ribosome. In addition, stalling mH-segments allow for insertion of the following transmembrane segment, forming an Ncytosol/Clumen orientation, suggesting that mH-segments can move laterally to accommodate the next transmembrane segment. These findings suggest that mH-segments may be accommodated at the ER membrane with lateral fluctuation between the Sec61 channel and the lipid phase.

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