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Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

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Standard

Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. / Schmüser, L; Trefz, M; Roeters, S J et al.

I: Langmuir : the ACS journal of surfaces and colloids, Bind 37, Nr. 45, 11.2021, s. 13452-13459.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Schmüser, L, Trefz, M, Roeters, SJ, Beckner, W, Pfaendtner, J, Otzen, D, Woutersen, S, Bonn, M, Schneider, D & Weidner, T 2021, 'Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy', Langmuir : the ACS journal of surfaces and colloids, bind 37, nr. 45, s. 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

APA

Schmüser, L., Trefz, M., Roeters, S. J., Beckner, W., Pfaendtner, J., Otzen, D., Woutersen, S., Bonn, M., Schneider, D., & Weidner, T. (2021). Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids, 37(45), 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

CBE

Schmüser L, Trefz M, Roeters SJ, Beckner W, Pfaendtner J, Otzen D, Woutersen S, Bonn M, Schneider D, Weidner T. 2021. Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids. 37(45):13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

MLA

Schmüser, L et al. "Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy". Langmuir : the ACS journal of surfaces and colloids. 2021, 37(45). 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

Vancouver

Schmüser L, Trefz M, Roeters SJ, Beckner W, Pfaendtner J, Otzen D et al. Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. Langmuir : the ACS journal of surfaces and colloids. 2021 nov.;37(45):13452-13459. Epub 2021 nov. 3. doi: 10.1021/acs.langmuir.1c02206

Author

Schmüser, L ; Trefz, M ; Roeters, S J et al. / Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. I: Langmuir : the ACS journal of surfaces and colloids. 2021 ; Bind 37, Nr. 45. s. 13452-13459.

Bibtex

@article{2e83d6f376574187a4f064b2acbff1a7,
title = "Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy",
abstract = "High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF), an aquaporin membrane channel finely tuned to selectively transport water and glycerol molecules across the membrane barrier. We find subtle but significant differences between the XRD structure and the inferred in situ structure of GlpF.",
keywords = "BILAYER, CHANNEL, CRYSTAL, GLYCEROL, INTERFACE, MOLECULAR-DYNAMICS, ORIENTATION, PEPTIDE, PROTEIN, VIBRATIONAL SPECTROSCOPY",
author = "L Schm{\"u}ser and M Trefz and Roeters, {S J} and W Beckner and J Pfaendtner and D Otzen and S Woutersen and M Bonn and D Schneider and T Weidner",
year = "2021",
month = nov,
doi = "10.1021/acs.langmuir.1c02206",
language = "English",
volume = "37",
pages = "13452--13459",
journal = "Langmuir",
issn = "0743-7463",
publisher = "AMER CHEMICAL SOC",
number = "45",

}

RIS

TY - JOUR

T1 - Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

AU - Schmüser, L

AU - Trefz, M

AU - Roeters, S J

AU - Beckner, W

AU - Pfaendtner, J

AU - Otzen, D

AU - Woutersen, S

AU - Bonn, M

AU - Schneider, D

AU - Weidner, T

PY - 2021/11

Y1 - 2021/11

N2 - High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF), an aquaporin membrane channel finely tuned to selectively transport water and glycerol molecules across the membrane barrier. We find subtle but significant differences between the XRD structure and the inferred in situ structure of GlpF.

AB - High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF), an aquaporin membrane channel finely tuned to selectively transport water and glycerol molecules across the membrane barrier. We find subtle but significant differences between the XRD structure and the inferred in situ structure of GlpF.

KW - BILAYER

KW - CHANNEL

KW - CRYSTAL

KW - GLYCEROL

KW - INTERFACE

KW - MOLECULAR-DYNAMICS

KW - ORIENTATION

KW - PEPTIDE

KW - PROTEIN

KW - VIBRATIONAL SPECTROSCOPY

UR - http://www.scopus.com/inward/record.url?scp=85118969452&partnerID=8YFLogxK

U2 - 10.1021/acs.langmuir.1c02206

DO - 10.1021/acs.langmuir.1c02206

M3 - Journal article

C2 - 34729987

VL - 37

SP - 13452

EP - 13459

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 45

ER -