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spelling paper:paper_00222631_v251_n5-6_p609_Friedman2023-06-08T14:48:40Z Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology Cell membrane Computational biophysics Lipid–protein interactions Molecular dynamics amylin cholesterol dopamine transporter epidermal growth factor receptor fat droplet glucose transporter 1 lipid thylakoid membrane protein biomembrane cell membrane crystal structure glucose transport high temperature hormone binding human lipid composition lipid membrane lipid raft molecular dynamics nonhuman protein conformation protein degradation protein interaction protein localization protein protein interaction Review temperature sensitivity This is a perspective article entitled “Frontiers in computational biophysics: understanding conformational dynamics of complex lipid mixtures relevant to biology” which is following a CECAM meeting with the same name. Graphical Abstract: [Figure not available: see fulltext.]. © 2018, The Author(s). 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222631_v251_n5-6_p609_Friedman http://hdl.handle.net/20.500.12110/paper_00222631_v251_n5-6_p609_Friedman
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cell membrane
Computational biophysics
Lipid–protein interactions
Molecular dynamics
amylin
cholesterol
dopamine transporter
epidermal growth factor receptor
fat droplet
glucose transporter 1
lipid
thylakoid membrane protein
biomembrane
cell membrane
crystal structure
glucose transport
high temperature
hormone binding
human
lipid composition
lipid membrane
lipid raft
molecular dynamics
nonhuman
protein conformation
protein degradation
protein interaction
protein localization
protein protein interaction
Review
temperature sensitivity
spellingShingle Cell membrane
Computational biophysics
Lipid–protein interactions
Molecular dynamics
amylin
cholesterol
dopamine transporter
epidermal growth factor receptor
fat droplet
glucose transporter 1
lipid
thylakoid membrane protein
biomembrane
cell membrane
crystal structure
glucose transport
high temperature
hormone binding
human
lipid composition
lipid membrane
lipid raft
molecular dynamics
nonhuman
protein conformation
protein degradation
protein interaction
protein localization
protein protein interaction
Review
temperature sensitivity
Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
topic_facet Cell membrane
Computational biophysics
Lipid–protein interactions
Molecular dynamics
amylin
cholesterol
dopamine transporter
epidermal growth factor receptor
fat droplet
glucose transporter 1
lipid
thylakoid membrane protein
biomembrane
cell membrane
crystal structure
glucose transport
high temperature
hormone binding
human
lipid composition
lipid membrane
lipid raft
molecular dynamics
nonhuman
protein conformation
protein degradation
protein interaction
protein localization
protein protein interaction
Review
temperature sensitivity
description This is a perspective article entitled “Frontiers in computational biophysics: understanding conformational dynamics of complex lipid mixtures relevant to biology” which is following a CECAM meeting with the same name. Graphical Abstract: [Figure not available: see fulltext.]. © 2018, The Author(s).
title Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
title_short Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
title_full Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
title_fullStr Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
title_full_unstemmed Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology
title_sort understanding conformational dynamics of complex lipid mixtures relevant to biology
publishDate 2018
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222631_v251_n5-6_p609_Friedman
http://hdl.handle.net/20.500.12110/paper_00222631_v251_n5-6_p609_Friedman
_version_ 1768541644362088448