scholarly journals Lipid Head Group Parameterization for GROMOS 54A8: A Consistent Approach with Protein Force Field Description

2019 ◽  
Vol 15 (10) ◽  
pp. 5175-5193
Author(s):  
Irene Marzuoli ◽  
Christian Margreitter ◽  
Franca Fraternali
Keyword(s):  
Force Field ◽  
Head Group ◽  
Lipid Head Group ◽  
Consistent Approach

scholarly journals Correction: Effect of lipid head group interactions on membrane properties and membrane-induced cationic β-hairpin folding

2016 ◽  
Vol 18 (38) ◽  
pp. 26998-26998
Author(s):  
Sai J. Ganesan ◽  
Hongcheng Xu ◽  
Silvina Matysiak
Keyword(s):  
Chem Phys ◽  
Membrane Properties ◽  
Head Group ◽  
Group Interactions ◽  
Correction Effect ◽  
Lipid Head Group ◽  
Phys Chem Chem Phys

Correction for ‘Effect of lipid head group interactions on membrane properties and membrane-induced cationic β-hairpin folding’ by Sai J. Ganesan et al., Phys. Chem. Chem. Phys., 2016, 18, 17836–17850.

scholarly journals How Transmembrane Model Peptides Affect Lipid Head Group Orientation: An Application of 14N NMR

2011 ◽  
Vol 100 (3) ◽  
pp. 638a-639a ◽  
Author(s):  
Jacques P.F. Doux ◽  
Benjamin A. Hall ◽  
J. Antoinette Killian
Keyword(s):  
Head Group ◽  
Group Orientation ◽  
Lipid Head Group ◽  
14N Nmr ◽  
Model Peptides

scholarly journals Internalization of Phospholipids from the Plasma Membrane of Human Osteoblasts Depends on the Lipid Head Group

1999 ◽  
Vol 14 (5) ◽  
pp. 690-699 ◽  
Author(s):  
Jeanette Libera ◽  
Thomas Pomorski ◽  
Oliviera Josimović-Alasević ◽  
Karl-Gerd Fritsch ◽  
Andreas Herrmann
Keyword(s):  
Plasma Membrane ◽  
Head Group ◽  
Human Osteoblasts ◽  
Lipid Head Group

Temperature- and ionic strength-induced conformational changes in the lipid head group region of liposomes as suggested by zeta potential data

1991 ◽  
Vol 41 (2) ◽  
pp. 175-183 ◽  
Author(s):  
Kimiko Makino ◽  
Takeshi Yamada ◽  
Mariko Kimura ◽  
Takashi Oka ◽  
Hiroyuki Ohshima ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Zeta Potential ◽  
Conformational Changes ◽  
Head Group ◽  
Lipid Head Group

On the lipid head group hydration of floating surface monolayers bound to self-assembled molecular protein layers

1994 ◽  
Vol 242 (1-2) ◽  
pp. 112-117 ◽  
Author(s):  
Mathias Lösche ◽  
Christian Erdelen ◽  
Elmar Rump ◽  
Helmut Ringsdorf ◽  
Kristian Kjaer ◽  
...  
Keyword(s):  
Head Group ◽  
Self Assembled ◽  
Lipid Head Group ◽  
Surface Monolayers ◽  
Floating Surface

scholarly journals Lipid Influence on the Structure of the Light Harvesting B 800—850 Proteins

1987 ◽  
Vol 42 (1-2) ◽  
pp. 109-117
Author(s):  
Joachim Peschke ◽  
Helmuth Möhwald
Keyword(s):  
Phase State ◽  
Transient Absorption ◽  
Photosynthetic Bacterium ◽  
Head Group ◽  
Lipid Phase ◽  
Elastic Model ◽  
Structural Protein ◽  
Protein Change ◽  
Lipid Environment ◽  
Lipid Head Group

Abstract Interaction of the antenna protein B 800-850 with the lipid environment and with the reaction center of the photosynthetic bacterium Rhodopseudomonas sphaeroides is studied by fluorescence spectroscopy, transient absorption techniques, light scattering and electron microscopy. Using vesicles of synthetic phospholipids it is shown that solidification of the m em brane causes a structural protein change evident from a reduction in fluorescence quantum yield. The change occurs at a tem perature up to 5 °C below that corresponding to the gel/fluid transition tem perature and indicates local melting. The structural change is not specific for the lipid head group nor chain length (investigated for lengths of 12 to 16 CH2 groups) and can be understood applying a simple elastic model. It can also be included isothermally by changing the ionic milied and thus varying the lipid phase state. Energy transfer LHCP→RC is proven to be highly efficient in model m em branes and is not affected by the existence of a phase transition. This indicates two LHCP fractions one tightly - and one non-bound to the RC.

scholarly journals The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase

2019 ◽  
Vol 476 (5) ◽  
pp. 783-794 ◽  
Author(s):  
Lisa Theorin ◽  
Kristina Faxén ◽  
Danny Mollerup Sørensen ◽  
Rebekka Migotti ◽  
Gunnar Dittmar ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Substrate Recognition ◽  
Hydrolytic Activity ◽  
Head Group ◽  
Structural Element ◽  
Type Iv ◽  
Acyl Chains ◽  
Lipid Head Group ◽  
Phospholipid Transport ◽  
P Type

Abstract Type IV P-type ATPases (P4 ATPases) are lipid flippases that catalyze phospholipid transport from the exoplasmic to the cytoplasmic leaflet of cellular membranes, but the mechanism by which they recognize and transport phospholipids through the lipid bilayer remains unknown. In the present study, we succeeded in purifying recombinant aminophospholipid ATPase 2 (ALA2), a member of the P4 ATPase subfamily in Arabidopsis thaliana, in complex with the ALA-interacting subunit 5 (ALIS5). The ATP hydrolytic activity of the ALA2–ALIS5 complex was stimulated in a highly specific manner by phosphatidylserine. Small changes in the stereochemistry or the functional groups of the phosphatidylserine head group affected enzymatic activity, whereas alteration in the length and composition of the acyl chains only had minor effects. Likewise, the enzymatic activity of the ALA2–ALIS5 complex was stimulated by both mono- and di-acyl phosphatidylserines. Taken together, the results identify the lipid head group as the key structural element for substrate recognition by the P4 ATPase.

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