Efficient Quantification of Lipid Packing Defect Sensing by Amphipathic Peptides: Comparing Martini 2 and 3 with CHARMM36-Reference-Cited by-同舟云学术

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Efficient Quantification of Lipid Packing Defect Sensing by Amphipathic Peptides: Comparing Martini 2 and 3 with CHARMM36

Published:2022-06-16 Issue:7 Volume:18 Page:4503-4514
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

van Hilten Niek¹^ORCID,Stroh Kai Steffen²³^ORCID,Risselada Herre Jelger¹²³^ORCID

Affiliation:

1. Leiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The Netherlands

2. Department of Physics, Technical University Dortmund, Dortmund 44221, Germany

3. Institute for Theoretical Physics, Georg-August-University Göttingen, Göttingen 37077, Germany

Funder

Deutsche Forschungsgemeinschaft

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.2c00222

Reference50 articles.

1. How curved membranes recruit amphipathic helices and protein anchoring motifs

2. A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

3. α-Synuclein Senses Lipid Packing Defects and Induces Lateral Expansion of Lipids Leading to Membrane Remodeling

4. Stressed Lipid Droplets: How Neutral Lipids Relieve Surface Tension and Membrane Expansion Drives Protein Association

5. The Many Faces of Amphipathic Helices

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