Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly

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Understanding and modelling the interactions of peptides with membranes : from partitioning to self-assembly. / Chen, Charles H.; Melo, Marcelo CR; Berglund, Nils; Khan, Ayesha; de la Fuente, César; Ulmschneider, Jakob P.; Ulmschneider, Martin B.

I: Current Opinion in Structural Biology, Bind 61, 04.2020, s. 160-166.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

Harvard

Chen, CH, Melo, MCR, Berglund, N, Khan, A, de la Fuente, C, Ulmschneider, JP & Ulmschneider, MB 2020, 'Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly', Current Opinion in Structural Biology, bind 61, s. 160-166. https://doi.org/10.1016/j.sbi.2019.12.021

APA

Chen, C. H., Melo, M. CR., Berglund, N., Khan, A., de la Fuente, C., Ulmschneider, J. P., & Ulmschneider, M. B. (2020). Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly. Current Opinion in Structural Biology, 61, 160-166. https://doi.org/10.1016/j.sbi.2019.12.021

CBE

Chen CH, Melo MCR, Berglund N, Khan A, de la Fuente C, Ulmschneider JP, Ulmschneider MB. 2020. Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly. Current Opinion in Structural Biology. 61:160-166. https://doi.org/10.1016/j.sbi.2019.12.021

MLA

Vancouver

Chen CH, Melo MCR, Berglund N, Khan A, de la Fuente C, Ulmschneider JP o.a. Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly. Current Opinion in Structural Biology. 2020 apr;61:160-166. https://doi.org/10.1016/j.sbi.2019.12.021

Author

Chen, Charles H. ; Melo, Marcelo CR ; Berglund, Nils ; Khan, Ayesha ; de la Fuente, César ; Ulmschneider, Jakob P. ; Ulmschneider, Martin B. / Understanding and modelling the interactions of peptides with membranes : from partitioning to self-assembly. I: Current Opinion in Structural Biology. 2020 ; Bind 61. s. 160-166.

Bibtex

@article{92bc08886ad44f478d83f809dcc65862,
title = "Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly",
abstract = "Atomic detail simulations are starting to reveal how flexible polypeptides interact with fluid lipid bilayers. These insights are transforming our understanding of one of the fundamental processes in biology: membrane protein folding and assembly. Advanced molecular dynamics (MD) simulation techniques enable accurate prediction of protein structure, folding pathways and assembly in microsecond-timescales. Such simulations show how membrane-active peptides self-assemble in cell membranes, revealing their binding, folding, insertion, and aggregation, while at the same time providing atomic resolution details of peptide–lipid interactions. Essential to the impact of simulations are experimental approaches that enable calibration and validation of the computational models and techniques. In this review, we summarize the current development of applying unbiased atomic detail MD simulations and the relation to experimental techniques, to study peptide folding and provide our perspective of the field.",
author = "Chen, {Charles H.} and Melo, {Marcelo CR} and Nils Berglund and Ayesha Khan and {de la Fuente}, C{\'e}sar and Ulmschneider, {Jakob P.} and Ulmschneider, {Martin B.}",
year = "2020",
month = apr,
doi = "10.1016/j.sbi.2019.12.021",
language = "English",
volume = "61",
pages = "160--166",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Understanding and modelling the interactions of peptides with membranes

T2 - from partitioning to self-assembly

AU - Chen, Charles H.

AU - Melo, Marcelo CR

AU - Berglund, Nils

AU - Khan, Ayesha

AU - de la Fuente, César

AU - Ulmschneider, Jakob P.

AU - Ulmschneider, Martin B.

PY - 2020/4

Y1 - 2020/4

N2 - Atomic detail simulations are starting to reveal how flexible polypeptides interact with fluid lipid bilayers. These insights are transforming our understanding of one of the fundamental processes in biology: membrane protein folding and assembly. Advanced molecular dynamics (MD) simulation techniques enable accurate prediction of protein structure, folding pathways and assembly in microsecond-timescales. Such simulations show how membrane-active peptides self-assemble in cell membranes, revealing their binding, folding, insertion, and aggregation, while at the same time providing atomic resolution details of peptide–lipid interactions. Essential to the impact of simulations are experimental approaches that enable calibration and validation of the computational models and techniques. In this review, we summarize the current development of applying unbiased atomic detail MD simulations and the relation to experimental techniques, to study peptide folding and provide our perspective of the field.

AB - Atomic detail simulations are starting to reveal how flexible polypeptides interact with fluid lipid bilayers. These insights are transforming our understanding of one of the fundamental processes in biology: membrane protein folding and assembly. Advanced molecular dynamics (MD) simulation techniques enable accurate prediction of protein structure, folding pathways and assembly in microsecond-timescales. Such simulations show how membrane-active peptides self-assemble in cell membranes, revealing their binding, folding, insertion, and aggregation, while at the same time providing atomic resolution details of peptide–lipid interactions. Essential to the impact of simulations are experimental approaches that enable calibration and validation of the computational models and techniques. In this review, we summarize the current development of applying unbiased atomic detail MD simulations and the relation to experimental techniques, to study peptide folding and provide our perspective of the field.

UR - http://www.scopus.com/inward/record.url?scp=85078461031&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2019.12.021

DO - 10.1016/j.sbi.2019.12.021

M3 - Review

C2 - 32006812

AN - SCOPUS:85078461031

VL - 61

SP - 160

EP - 166

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

ER -