[NMR paper] Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy
Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy
Understanding how the amino acid sequence dictates protein structure and defines its stability is a fundamental problem in molecular biology. It is especially challenging for membrane proteins that reside in the complex environment of a lipid bilayer. Here, we obtain an atomic-level picture of the thermally induced unfolding of a membrane-embedded ?-helical protein, human aquaporin 1, using solid-state nuclear magnetic resonance spectroscopy. Our data reveal the hierarchical two-step...
[NMR paper] Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
J Phys Chem B. 2017 Apr 13;:
Authors: Gopinath T, Nelson SE, Soller KJ, Veglia G
Abstract
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 states, are sparsely...
[NMR paper] Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Publication date: Available online 25 August 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Jonathan K. Williams , Mei Hong</br>
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected 1H polarization transfer from water to biomolecules is a versatile approach for studying water-protein, water-membrane, and water-carbohydrate interactions in biology. We review...