Paramagnetic chemical probes for studying biological macromolecules

Q Miao, C Nitsche, H Orton, M Overhand… - Chemical …, 2022 - ACS Publications
Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

Investigating protein–ligand interactions by solution nuclear magnetic resonance spectroscopy

W Becker, KC Bhattiprolu, N Gubensäk… - …, 2018 - Wiley Online Library
Protein–ligand interactions are of fundamental importance in almost all processes in living
organisms. The ligands comprise small molecules, drugs or biological macromolecules and …

Structure and inhibition of the SARS coronavirus envelope protein ion channel

K Pervushin, E Tan, K Parthasarathy, X Lin… - PLoS …, 2009 - journals.plos.org
The envelope (E) protein from coronaviruses is a small polypeptide that contains at least
one α-helical transmembrane domain. Absence, or inactivation, of E protein results in …

NMR approaches for structural analysis of multidomain proteins and complexes in solution

C Göbl, T Madl, B Simon, M Sattler - Progress in Nuclear Magnetic …, 2014 - Elsevier
NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

[HTML][HTML] Simplifying proton NMR spectra by instant homonuclear broadband decoupling

NH Meyer, K Zangger - Angewandte Chemie (International ed. in …, 2013 - ncbi.nlm.nih.gov
NMR spectroscopy is a versatile tool to determine structural, chemical, and physical
properties of molecules. One-dimensional 1H NMR spectra probably represent the most …

Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects

J Koehler, J Meiler - Progress in nuclear magnetic resonance spectroscopy, 2011 - Elsevier
NMR spectroscopy is one of the most important methods for determining protein structures.
The scientific community is constantly pushing the limits of NMR spectroscopy by …

[HTML][HTML] Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function

S Welker, B Rudolph, E Frenzel, F Hagn, G Liebisch… - Molecular cell, 2010 - cell.com
Hsp12 of S. cerevisiae is upregulated several 100-fold in response to stress. Our phenotypic
analysis showed that this protein is important for survival of a variety of stress conditions …

A novel chimeric cell-penetrating peptide with membrane-disruptive properties for efficient endosomal escape

F Salomone, F Cardarelli, M Di Luca, C Boccardi… - Journal of controlled …, 2012 - Elsevier
Efficient endocytosis into a wide range of target cells and low toxicity make the arginine-rich
Tat peptide (Tat11: YGRKKRRQRRR, residues 47–57 of HIV-1 Tat protein) an excellent …

[HTML][HTML] Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?

EF Haney, HN Hunter, K Matsuzaki, HJ Vogel - Biochimica et Biophysica …, 2009 - Elsevier
The high-resolution three-dimensional structure of an antimicrobial peptide has implications
for the mechanism of its antimicrobial activity, as the conformation of the peptide provides …

Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol

E Teissier, G Zandomeneghi, A Loquet, D Lavillette… - PloS one, 2011 - journals.plos.org
The broad-spectrum antiviral arbidol (Arb) inhibits cell entry of enveloped viruses by
blocking viral fusion with host cell membrane. To better understand Arb mechanism of …