Transmembrane α helices

Mall, Sanjay; East, J. Malcolm; Lee, Anthony G.

doi:10.1016/s1063-5823(02)52014-7

Cited by 4 publications

(1 citation statement)

References 97 publications

(130 reference statements)

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“…For example, when reconstituted into synthetic membranes of differing thickness, Ca 2+ -ATPase and (Na + ,K + )-ATPase display maximum activity when the lipid acyl chains are 18C in length. 54 The effects of peptide-lipid interactions, both on the properties of bilayers and the activity of membrane proteins, have therefore received much scrutiny. Hydrophobic mismatch, 55 in which the length of the hydrophobic region of the peptide is different to the diameter of the hydrophobic interior of the membrane, has been examined intensively using helical peptides.…”

Section: Helical Peptide Models For Integral Membrane Proteinsmentioning

confidence: 99%

Peptide—Lipid Interactions: Insights and Perspectives

Sanderson

2005

ChemInform

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Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. This submission was created using the RSC Article Template (DO NOT DELETE THIS TEXT) (LINE INCLUDED FOR SPACING ONLY -DO NOT DELETE THIS TEXT)As the number of membrane proteins in the Protein Data Bank increases, efforts to understand how they interact with their natural environment are increasing in importance. A number of membrane proteins crystallise with lipid molecules implicitly bound at discrete locations that are consistent with the transmembrane regions of the protein. Bioinformatics studies also point to the specific interactions of some amino acids with membrane lipids. The results of experiments using model systems are revealing how these interactions contribute to the stability of both the protein and the membrane in which it is embedded. From a different perspective, the processes involved in the binding of peptides to membrane surfaces to produce a variety of effects are being understood in ever-increasing detail. This review describes current research efforts and thinking in this area.

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Section: Helical Peptide Models For Integral Membrane Proteinsmentioning

confidence: 99%

Peptide—Lipid Interactions: Insights and Perspectives

Sanderson

2005

ChemInform

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On the role of anionic lipids in charged protein interactions with membranes

Vorobyov

Allen

2011

Biochimica et Biophysica Acta (BBA) - Biomembranes

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We investigate the role of anionic lipids in the binding to, and subsequent movement of charged protein groups in lipid membranes, to help understand the role of membrane composition in all membrane-active protein sequences. We demonstrate a small effect of phosphatidylglycerol (PG) lipids on the ability of an arginine (Arg) side chain to bind to, and cross a lipid membrane, despite possessing a neutralizing charge. We observe similar membrane deformations in lipid bilayers composed of phosphatidylcholine (PC) and PC/PG mixtures, with comparable numbers of water and lipid head groups pulled into the bilayer hydrocarbon core, and prohibitively large ~20 kcal/mol barriers for Arg transfer across each bilayer, dropping by just 2-3 kcal/mol due to the binding of PG lipids. We explore the causes of this small effect of introducing PG lipids and offer an explanation in terms of the limited membrane interaction for the choline groups of PC lipids bound to the translocating ion. Our calculations reveal a surprising lack of preference for Arg binding to PG lipids themselves, but a small increase in interfacial binding affinity for lipid bilayers containing PG lipids. These results help to explain the nature of competitive lipid binding to charged protein sequences, with implications for a wide range of membrane binding domains and cell perturbing peptides.

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Peptide–lipid interactions: insights and perspectives

Sanderson

2005

Org. Biomol. Chem.

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, J. M. (2005) 'Peptide-lipid interactions : insights and perspectives.', Organic biomolecular chemistry., 3 (2). pp. 201-212. Further information on publisher's website: http://dx. The full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that: • a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders. Please consult the full DRO policy for further details. This submission was created using the RSC Article Template (DO NOT DELETE THIS TEXT) (LINE INCLUDED FOR SPACING ONLY-DO NOT DELETE THIS TEXT) As the number of membrane proteins in the Protein Data Bank increases, efforts to understand how they interact with their natural environment are increasing in importance. A number of membrane proteins crystallise with lipid molecules implicitly bound at discrete locations that are consistent with the transmembrane regions of the protein. Bioinformatics studies also point to the specific interactions of some amino acids with membrane lipids. The results of experiments using model systems are revealing how these interactions contribute to the stability of both the protein and the membrane in which it is embedded. From a different perspective, the processes involved in the binding of peptides to membrane surfaces to produce a variety of effects are being understood in ever-increasing detail. This review describes current research efforts and thinking in this area.

show abstract

Transmembrane α helices

Cited by 4 publications

References 97 publications

Peptide—Lipid Interactions: Insights and Perspectives

Peptide—Lipid Interactions: Insights and Perspectives

On the role of anionic lipids in charged protein interactions with membranes

Peptide–lipid interactions: insights and perspectives

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