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

L Schmüser; M Trefz; S J Roeters; W Beckner; J Pfaendtner; D Otzen; S Woutersen; M Bonn; D Schneider; T Weidner

doi:10.1021/acs.langmuir.1c02206

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

L Schmüser, M Trefz, S J Roeters, W Beckner, J Pfaendtner, D Otzen, S Woutersen, M Bonn, D Schneider, T Weidner

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

4 Citations (Scopus)

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.

Original language	English
Journal	Langmuir : the ACS journal of surfaces and colloids
Volume	37
Issue	45
Pages (from-to)	13452-13459
Number of pages	8
ISSN	0743-7463
DOIs	https://doi.org/10.1021/acs.langmuir.1c02206
Publication status	Published - Nov 2021

Keywords

BILAYER
CHANNEL
CRYSTAL
GLYCEROL
INTERFACE
MOLECULAR-DYNAMICS
ORIENTATION
PEPTIDE
PROTEIN
VIBRATIONAL SPECTROSCOPY

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10.1021/acs.langmuir.1c02206

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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

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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 : the ACS journal of surfaces and colloids",

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}

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, vol. 37, no. 45, pp. 13452-13459. https://doi.org/10.1021/acs.langmuir.1c02206

Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy. / Schmüser, L; Trefz, M; Roeters, S J et al.
In: Langmuir : the ACS journal of surfaces and colloids, Vol. 37, No. 45, 11.2021, p. 13452-13459.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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

SN - 0743-7463

VL - 37

SP - 13452

EP - 13459

JO - Langmuir : the ACS journal of surfaces and colloids

JF - Langmuir : the ACS journal of surfaces and colloids

IS - 45

ER -

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

Abstract

Keywords

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