Role of disulfide linkages in tachyplesin-lipid interactions

Biochemistry ◽  
1993 ◽  
Vol 32 (43) ◽  
pp. 11704-11710 ◽  
Author(s):  
Katsumi Matsuzaki ◽  
Mitsuya Nakayama ◽  
Masaru Fukui ◽  
Akira Otaka ◽  
Susumu Funakoshi ◽  
...  
Keyword(s):  
Lipid Interactions ◽  
Disulfide Linkages

Contribution of hydrogen bonding to lipid-lipid interactions in membranes and the role of lipid order: Effects of cholesterol, increased phospholipid unsaturation, and ethanol

Biochemistry ◽  
1993 ◽  
Vol 32 (14) ◽  
pp. 3714-3721 ◽  
Author(s):  
Simon J. Slater ◽  
Cojen Ho ◽  
Frank J. Taddeo ◽  
Mary Beth Kelly ◽  
Christopher D. Stubbs
Keyword(s):  
Hydrogen Bonding ◽  
Order Effects ◽  
Lipid Interactions ◽  
Lipid Order

scholarly journals The Role of Lipid Interactions in Simulations of the α-Hemolysin Ion-Channel-Forming Toxin

2018 ◽  
Vol 115 (9) ◽  
pp. 1720-1730 ◽  
Author(s):  
Nicholas B. Guros ◽  
Arvind Balijepalli ◽  
Jeffery B. Klauda
Keyword(s):  
Ion Channel ◽  
Lipid Interactions

Novel role of pleckstrin homology domain of the Bcr-Abl protein: Analysis of protein–protein and protein–lipid interactions

2010 ◽  
Vol 316 (4) ◽  
pp. 530-542 ◽  
Author(s):  
Daria Miroshnychenko ◽  
Anna Dubrovska ◽  
Stanislav Maliuta ◽  
Gennady Telegeev ◽  
Pontus Aspenström
Keyword(s):  
Protein Analysis ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Lipid Interactions

scholarly journals The Role of Protein-Lipid Interactions in the Functioning of Bitopic Membrane Proteins

2020 ◽  
Vol 118 (3) ◽  
pp. 211a
Author(s):  
Eduard V. Bocharov ◽  
Dmitry M. Lesovoy ◽  
Olga V. Bocharova ◽  
Anatoly S. Urban ◽  
Yaroslav V. Bershacky ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lipid Interactions

Role of single disulfide linkages in the folding and activity of scyllatoxin-based BH3 domain mimetics

2017 ◽  
Vol 23 (5) ◽  
pp. 367-373 ◽  
Author(s):  
Danushka Arachchige ◽  
M. Margaret Harris ◽  
Zachary Coon ◽  
Jacob Carlsen ◽  
Justin M. Holub
Keyword(s):  
Bh3 Domain ◽  
Disulfide Linkages

scholarly journals Preservation of the native structure and function of Ca2+-ATPase from sarcoplasmic reticulum: Solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine

1997 ◽  
Vol 325 (2) ◽  
pp. 533-542 ◽  
Author(s):  
Bannikuppe D. SHIVANNA ◽  
Elizabeth S. ROWE
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Membrane Proteins ◽  
Conformational Transition ◽  
Specific Activity ◽  
Structure And Function ◽  
Native Structure ◽  
Lipid Interactions ◽  
Lauryl Ether ◽  
And Function

The properties of Ca2+-ATPase purified and reconstituted from rabbit skeletal sarcoplasmic reticulum (SR) has been studied in comparison with the preparations obtained by the commonly used detergent poly(oxyethylene)8-lauryl ether (C12E8) and the bile salt detergents cholate and deoxycholate. 1,2-Diheptanoyl-sn-phosphatidylcholine (DHPC) has been shown to be excellent for solubilizing a wide variety of membrane proteins [Kessi, Poiree, Wehrli, Bachofen, Semenza and Hauser (1994) Biochemistry 33, 10825–10836]. The DHPC method consistently gave higher yields of purified Ca2+-ATPase with a greater specific activity than the methods with C12E8, cholate, or deoxycholate. DHPC and C12E8 were superior to cholate and deoxycholate in active enzyme yields and specific activity. DHPC-solubilized Ca2+-ATPase purified on a density gradient retained the E1Ca–E1*Ca conformational transition, whereas the enzyme from the C12E8 purification did not retain this transition. The coupling of Ca2+ transported to ATP hydrolysed in the DHPC-purified enzyme was maximal and matched the values obtained with native SR, whereas the coupling was much lower for the C12E8-purified enzyme. The specific activity of Ca2+-ATPase reconstituted into dioleoylphosphatidylcholine vesicles with DHPC was up to 2-fold greater than that achieved with C12E8, and is comparable to that measured in the native SR. Finally, the dissociation of Ca2+-ATPase into monomers by DHPC preserved the ATPase activity, whereas similar dissociation by C12E8 gave only one-sixth the activity of that obtained with DHPC. These studies show that the Ca2+-ATPase solubilized, purified and reconstituted with DHPC is superior to that obtained with C12E8 in significant ways, making it a preparation suitable for detailed studies on the mechanism of ion transport and the role of protein–lipid interactions in the function of membrane proteins.

scholarly journals Control and role of pH in peptide–lipid interactions in oriented membrane samples

2015 ◽  
Vol 1848 (3) ◽  
pp. 833-841 ◽  
Author(s):  
Julia Misiewicz ◽  
Sergii Afonin ◽  
Anne S. Ulrich
Keyword(s):  
Lipid Interactions

The Role of Drug-Lipid Interactions on the Disposition of Liposome-Formulated Opioid Analgesics In Vitro and In Vivo

2001 ◽  
Vol 93 (4) ◽  
pp. 928-933 ◽  
Author(s):  
Claudette R. Bethune ◽  
Christopher M. Bernards ◽  
Tot Bui-Nguyen ◽  
Danny D. Shen ◽  
Rodney J. Y. Ho
Keyword(s):  
Opioid Analgesics ◽  
Lipid Interactions
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