Perturbations of native membrane protein structure in alkyl phosphocholine detergents: a critical assessment of NMR and biophysical studies

C Chipot, F Dehez, JR Schnell, N Zitzmann… - Chemical …, 2018 - ACS Publications
Membrane proteins perform a host of vital cellular functions. Deciphering the molecular
mechanisms whereby they fulfill these functions requires detailed biophysical and structural …

Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban

M Gustavsson, R Verardi, DG Mullen… - Proceedings of the …, 2013 - National Acad Sciences
The membrane protein complex between the sarcoplasmic reticulum Ca2+-ATPase
(SERCA) and phospholamban (PLN) controls Ca2+ transport in cardiomyocytes, thereby …

Probing membrane protein ground and conformationally excited states using dipolar-and J-coupling mediated MAS solid state NMR experiments

T Gopinath, G Veglia - Methods, 2018 - Elsevier
The intrinsic conformational plasticity of membrane proteins directly influences the
magnitude of the orientational-dependent NMR interactions such as dipolar couplings (DC) …

Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport

VV Vostrikov, KR Mote, R Verardi, G Veglia - Structure, 2013 - cell.com
Phospholamban (PLN) inhibits the sarco (endo) plasmic reticulum Ca 2+-ATPase (SERCA),
thereby regulating cardiac diastole. In membranes, PLN assembles into homopentamers …

[HTML][HTML] Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions

VV Vostrikov, KJ Soller, KN Ha, T Gopinath… - Biochimica et Biophysica …, 2015 - Elsevier
Phospholamban (PLN) is a single-pass membrane protein that regulates the sarco (endo)
plasmic reticulum Ca 2+-ATPase (SERCA). Phosphorylation of PLN at Ser16 reverses its …

Proton-detected polarization optimized experiments (POE) using ultrafast magic angle spinning solid-state NMR: Multi-acquisition of membrane protein spectra

T Gopinath, G Veglia - Journal of Magnetic Resonance, 2020 - Elsevier
Proton-detected solid-state NMR (ssNMR) spectroscopy has dramatically improved the
sensitivity and resolution of fast magic angle spinning (MAS) methods. While relatively …

Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation

A De Simone, M Gustavsson, RW Montalvao, L Shi… - Biochemistry, 2013 - ACS Publications
Phospholamban is an integral membrane protein that controls the calcium balance in
cardiac muscle cells. As the function and regulation of this protein require the active …

[HTML][HTML] Effects of the Arg9Cys and Arg25Cys mutations on phospholamban's conformational equilibrium in membrane bilayers

SED Nelson, KN Ha, T Gopinath, MH Exline… - … et Biophysica Acta (BBA …, 2018 - Elsevier
Abstract Approximately, 70% of the Ca 2+ ion transport into the sarcoplasmic reticulum is
catalyzed by the sarcoplasmic reticulum Ca 2+-ATPase (SERCA), whose activity is …

Probing the Conformationally Excited States of Membrane Proteins via 1H-Detected MAS Solid-State NMR Spectroscopy

T Gopinath, SED Nelson, KJ Soller… - The Journal of Physical …, 2017 - ACS Publications
Proteins exist in ensembles of conformational states that interconvert on various motional
time scales. High-energy states of proteins, often referred to as conformationally excited …

Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations

A De Simone, KR Mote, G Veglia - Biophysical journal, 2014 - cell.com
Solid-state NMR spectroscopy is emerging as a powerful approach to determine structure,
topology, and conformational dynamics of membrane proteins at the atomic level …