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

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 -