Differential Binding Affinities and Allosteric Conformational Changes Underlie Interactions of Yorkie and a Multivalent PPxY Partner. Targeting Alanines in the Hydrophobic and Cross-Linking Domains of Native Elastin with Isotopic Enrichment and Solid-State NMR Spectroscopy. Jhonsen Djajamuliadi, Kosuke Ohgo, Kristin K.Solid-State NMR Spectroscopy and Isotopic Labeling Target Abundant Dipeptide Sequences in Elastin’s Hydrophobic Domains. The Journal of Physical Chemistry B 2018, 122 Generating Intrinsically Disordered Protein Conformational Ensembles from a Database of Ramachandran Space Pair Residue Probabilities Using a Markov Chain. Journal of the American Chemical Society 2018, 140 The Singular NMR Fingerprint of a Polyproline II Helical Bundle. Victoria Gomez, Miguel Mompeán, Douglas V. Ángel Treviño, David Pantoja-Uceda, Margarita Menéndez, M. Detection of Labile Conformations of Elastin’s Prolines by Solid-State Nuclear Magnetic Resonance and Fourier Transform Infrared Techniques. Unambiguous Identification of Pyroglutamate in Full-Length Biopharmaceutical Monoclonal Antibodies by NMR Spectroscopy. Arthur Hinterholzer, Vesna Stanojlovic, Chiara Cabrele, Mario Schubert.Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy. Arthur Hinterholzer, Vesna Stanojlovic, Christof Regl, Christian G.The Journal of Organic Chemistry 2021, 86 Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops. Richaud, Guangkuan Zhao, Samir Hobloss, Stéphane P. Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A. 13C Direct Detected NMR for Challenging Systems.
Solid-State NMR Dipolar and Chemical Shift Anisotropy Recoupling Techniques for Structural and Dynamical Studies in Biological Systems. Lixin Liang, Yi Ji, Kuizhi Chen, Pan Gao, Zhenchao Zhao, Guangjin Hou.This article is cited by 483 publications. This new set of correction factors will have important applications to folded proteins as well as to short, unstructured peptides and unfolded proteins. The work includes a validation of the concepts used to derive sequence-dependent correction factors for random coil chemical shifts, and a comprehensive tabulation of sequence-dependent correction factors that can be applied for amino acids up to two residues from a given position. We present a detailed, quantitative analysis of the effect of the 20 naturally occurring amino acids on the random coil shifts of 15N H, 1H N, and 13CO resonances of neighboring residues, utilizing complete resonance assignments for a set of five-residue peptides Ac-G-G-X-G-G-NH 2. In particular, the amide nitrogen, amide proton, and carbonyl carbon chemical shifts are highly sensitive to the local amino acid sequence. While some of these deviations can be ascribed to residual structure in the unfolded protein, others are clearly caused by local sequence effects. While this technique is very reliable for folded proteins, application to unfolded proteins reveals significant deviations from measured random coil shifts for certain nuclei. Random coil chemical shifts are commonly used to detect secondary structure elements in proteins in chemical shift index calculations.
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