13C Direct Detected NMR for Challenging Systems

IC Felli, R Pierattelli - Chemical Reviews, 2022 - ACS Publications
Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design,
modern 13C NMR has become a useful tool for biomolecular applications. The complete …

NMR methods for the study of instrinsically disordered proteins structure, dynamics, and interactions: general overview and practical guidelines

B Brutscher, IC Felli, S Gil-Caballero, T Hošek… - … proteins studied by …, 2015 - Springer
Thanks to recent improvements in NMR instrumentation, pulse sequence design, and
sample preparation, a panoply of new NMR tools has become available for atomic …

Quantification of PDZ domain specificity, prediction of ligand affinity and rational design of super-binding peptides

U Wiedemann, P Boisguerin, R Leben, D Leitner… - Journal of molecular …, 2004 - Elsevier
Transient macromolecular complexes are often formed by protein–protein interaction
domains (eg PDZ, SH2, SH3, WW) which recognize linear sequence motifs with in vitro …

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA

T Madl, L Van Melderen, N Mine, M Respondek… - Journal of molecular …, 2006 - Elsevier
Toxin–antitoxin systems are highly abundant in plasmids and bacterial chromosomes. They
ensure plasmid maintenance by killing bacteria that have lost the plasmid. Their expression …

Automated structure determination of proteins by NMR spectroscopy

W Gronwald, HR Kalbitzer - Progress in Nuclear Magnetic Resonance …, 2004 - Elsevier
Contents 1. Introduction............................................................................. 33 1.1. Automated
structure determination methods in the postgenomics area.............................. 34 2. Automated …

PACES: protein sequential assignment by computer-assisted exhaustive search

BE Coggins, P Zhou - Journal of biomolecular NMR, 2003 - Springer
A crucial step in determining solution structures of proteins using nuclear magnetic
resonance (NMR) spectroscopy is the process of sequential assignment, which correlates …

NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation

V Slynko, M Schubert, S Numao… - Journal of the …, 2009 - ACS Publications
Although there is great interest in three-dimensional structures of glycoproteins and complex
oligosaccharides, their structural determination have been hampered by inhomogeneous …

Amino acid selective unlabeling for sequence specific resonance assignments in proteins

B Krishnarjuna, G Jaipuria, A Thakur, P D'Silva… - Journal of biomolecular …, 2011 - Springer
Sequence specific resonance assignment constitutes an important step towards high-
resolution structure determination of proteins by NMR and is aided by selective identification …

[HTML][HTML] Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein

P Agback, F Dominguez, Y Pustovalova, T Lukash… - Virology, 2019 - Elsevier
Alphavirus nsP3 proteins contain long, intrinsically disordered, hypervariable domains,
HVD, which serve as hubs for interaction with many cellular proteins. Here, we have …

Exclusively Heteronuclear 13C‐Detected Amino‐Acid‐Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs)

W Bermel, I Bertini, J Chill, IC Felli, N Haba… - …, 2012 - Wiley Online Library
Carbon‐13 direct‐detection NMR methods have proved to be very useful for the
characterization of intrinsically disordered proteins (IDPs). Here we present a suite of …