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 pathway...
[NMR paper] Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing Microenvironmental Acidity in Lyophilized Protein and Vaccine Formulations Using Solid-state NMR Spectroscopy.
J Pharm Sci. 2020 Nov 26;:
Authors: Li M, Koranne S, Fang R, Lu X, Williams DM, Munson EJ, Bhambhani A, Su Y
Abstract
Biophysical and biochemical...
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[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.
Related Articles Probing membrane protein structure using water polarization transfer solid-state NMR.
J Magn Reson. 2014 Aug 25;
Authors: Williams JK, Hong M
Abstract
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected (1)H polarization transfer from water to biomolecules is a versatile approach for studying water-protein,...
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[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...
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Related Articles Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Biochim Biophys Acta. 2010 Aug 15;
Authors: Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is...
Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy
Linear Mode
