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 [NMR paper] A lowly populated, transient ?-sheet structure in monomeric A?1-42 identified by multinuclear NMR of chemical denaturation. |
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Jan 18, 2021 - 7:42 AM - by nmrlearner
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A lowly populated, transient ?-sheet structure in monomeric A?1-42 identified by multinuclear NMR of chemical denaturation.
 Related Articles A lowly populated, transient ?-sheet structure in monomeric A?1-42 identified by multinuclear NMR of chemical denaturation.
Biophys Chem. 2020 Dec 24;270:106531
Authors: Kakeshpour T, Ramanujam V, Barnes CA, Shen Y, Ying J, Bax A
Abstract
Chemical denaturation is a well-established approach for probing the equilibrium between folded and unfolded states of proteins. We demonstrate applicability of this method to the detection of a small population of a transiently folded structural element in a system that is often considered to be intrinsically fully disordered. The 1HN, 15N, 13C?, and 13C' chemical shifts of A?1-40 and A?1-42 peptides and their M35-oxidized variants were monitored as a function of urea concentration and compared to analogous urea titrations of synthetic pentapeptides of homologous sequence. Fitting of the chemical shift titrations yields a 10*±*1% population for a... [Read More]
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0 Replies | 1 Views
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[NMR paper] Specificity of Molecular Fragments Binding to S100B versus S100A1 as Identified by NMR and Site Identification by Ligand Competitive Saturation (SILCS). |
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Jan 18, 2021 - 7:42 AM - by nmrlearner
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Specificity of Molecular Fragments Binding to S100B versus S100A1 as Identified by NMR and Site Identification by Ligand Competitive Saturation (SILCS).
Related Articles Specificity of Molecular Fragments Binding to S100B versus S100A1 as Identified by NMR and Site Identification by Ligand Competitive Saturation (SILCS).
Molecules. 2021 Jan 13;26(2):
Authors: Young BD, Yu W, Rodríguez DJV, Varney KM, MacKerell AD, Weber DJ
Abstract
S100B, a biomarker of malignant melanoma, interacts with the p53 protein and diminishes its tumor suppressor function, which makes this S100 family member a promising therapeutic target for treating malignant melanoma. However, it is a challenge to design inhibitors that are specific for S100B in melanoma versus other S100-family members that are important for normal cellular activities. For example, S100A1 is most similar in sequence and structure to S100B, and this S100 protein is important for normal skeletal and cardiac muscle function. Therefore, a combination of NMR and computer aided drug design (CADD) was used to initiate the design of specific S100B inhibitors. Fragment-based screening by NMR, also termed "SAR by NMR," is a well-established method, and was used to examine spectral perturbations in 2D [1H, 15N]-HSQC spectra of Ca2+-bound S100B and Ca2+-bound S100A1, side-by-side, and under identical conditions for comparison. Of the 1000 compounds... [Read More]
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0 Replies | 1 Views
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[NMR paper] Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins. |
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Jan 16, 2021 - 4:55 PM - by nmrlearner
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Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.
Related Articles Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.
Solid State Nucl Magn Reson. 2021 Jan 07;111:101710
Authors: Vugmeyster L
Abstract
Slow timescale dynamics in proteins are essential for a variety of biological functions spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as well as protein-protein and protein-nucleic acid interactions. In this review, we focus on the experimental and theoretical developments of 2H static NMR methods applicable for studies of microsecond to millisecond motional modes in proteins, particularly rotating frame relaxation dispersion (R1?), quadrupolar Carr-Purcell-Meiboom-Gill (QCPMG) relaxation dispersion, and quadrupolar chemical exchange saturation transfer NMR experiments (Q-CEST). With applications chosen from amyloid-? fibrils, we show the complementarity of these approaches for elucidating the complexities of conformational ensembles in disordered domains in the non-crystalline solid state, with the employment of selective deuterium labels. Combined with recent advances in relaxation dispersion backbone measurements for 15N/13C/1H nuclei, these techniques provide powerful tools for studies of biologically relevant timescale dynamics in disordered domains in the... [Read More]
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0 Replies | 7 Views
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[NMR paper] SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy. |
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Jan 16, 2021 - 4:55 PM - by nmrlearner
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SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
Related Articles SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
J Phys Chem B. 2021 Jan 15;:
Authors: Mendelman N, Meirovitch E
Abstract
We report on amide (N-H) NMR relaxation from the protein S100A1 analyzed with the slowly relaxing local structure (SRLS) approach. S100A1 comprises two calcium-binding "EF-hands" (helix-loop-helix motifs) connected by a linker. The dynamic structure of this protein, in both calcium-free and calcium-bound form, is described as the restricted local N-H motion coupled to isotropic protein tumbling. The restrictions are given by a rhombic potential, u (~10 kT), the local motion by a diffusion tensor with rate constant D2 (~109 s-1), and principal axis tilted from the N-H bond at angle ? (10-20°). This parameter combination provides a physically insightful picture of the dynamic structure of S100A1 from the N-H bond perspective. Calcium binding primarily affects the C-terminal EF-hand, among others slowing down the motion of helices III and IV approximately 10-fold. Overall, it brings about significant changes in the shape of the local potential, u, and the orientation of the local diffusion axis, ?. Conformational... [Read More]
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0 Replies | 7 Views
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[NMR paper] Laparoscopic sleeve gastrectomy alters 1H-NMR-measured lipoprotein and glycoprotein profile in patients with severe obesity and nonalcoholic fatty liver disease. |
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Jan 16, 2021 - 4:55 PM - by nmrlearner
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Laparoscopic sleeve gastrectomy alters 1H-NMR-measured lipoprotein and glycoprotein profile in patients with severe obesity and nonalcoholic fatty liver disease.
Related Articles Laparoscopic sleeve gastrectomy alters 1H-NMR-measured lipoprotein and glycoprotein profile in patients with severe obesity and nonalcoholic fatty liver disease.
Sci Rep. 2021 Jan 14;11(1):1343
Authors: Cabré N, Gil M, Amigó N, Luciano-Mateo F, Baiges-Gaya G, Fernández-Arroyo S, Rodríguez-Tomàs E, Hernández-Aguilera A, Castañé H, París M, Sabench F, Del Castillo D, Camps J, Joven J
Abstract
Patients with morbid obesity frequently present non-alcoholic fatty liver (NAFL) and non-alcoholic steatohepatitis (NASH) associated with pro-atherogenic alterations. Laparoscopic sleeve gastrectomy (LSG) is an effective treatment for weight reduction, and for the remission of hepatic alterations. Using 1H-nuclear magnetic resonance (1H-NMR), we investigated the effects of LSG on lipoprotein and glycoprotein profile in patients with morbid obesity and liver disease. We included 154 patients with morbid obesity (49 non-NASH, 54 uncertain NASH, 51 definite NASH). A blood sample was obtained before surgery and, in patients with definite NASH, one year after surgery. Patients with NASH had increased concentrations of medium and small VLDL particles, VLDL and IDL cholesterol concentrations, IDL, LDL, and HDL triglyceride... [Read More]
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