Fundamentals of protein NMR spectroscopy / за авторством 270690 Rule, Gordon S., Hitchens, T. Kevin

Protein NMR spectroscopy : principles and practice / за авторством Cavanagh, John, 1963-

Cell-free expression and selective isotope labelling in protein NMR. за авторством Staunton, D, Schlinkert, R, Zanetti, G, Colebrook, SA, Campbell, I

“...The availability of efficient cell-free expression systems with low levels of metabolic conversion allow the increasing use of selective isotope labelling as a tool in protein NMR. We describe two examples, one where a selective labelling scheme can identify backbone amide peaks from unassigned 1H--15N HSQC and HNCO spectra of a 84 residue protein, and another where a specific backbone amide in a 198 residue construct of the ninth and tenth Type III repeats from human fibronectin can be labelled and rapidly identified using a simple HSQC experiment....”

Assignment of protein NMR spectra using heteronuclear NMR: a tutorial за авторством Redfield, C

“...This chapter describes both the methodologies for protein NMR resonance assignment. Examples of how sequence specific resonance assignments can be obtained using a suite of 2D and 3D NMR experiments are presented and suggestions on how overlap problems can be overcome are included....”

Cooling overall spin temperature: protein NMR experiments optimized for longitudinal relaxation effects. за авторством Deschamps, M, Campbell, I

Polynomially scaling spin dynamics simulation algorithm based on adaptive state-space restriction. за авторством Kuprov, I, Wagner-Rundell, N, Hore, P

“...In cases of favourable interaction topologies (sparse graphs, e.g. in protein NMR) the asymptotic scaling is linear, opening the way to direct fitting of molecular structures to experimental spectra....”

The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases. за авторством Stammers, D, Ren, J, Leslie, K, Nichols, C, Lamb, H, Cocklin, S, Dodds, A, Hawkins, A

“...We show that NAD binds to NmrA, a previously unreported nucleotide binding property for this protein. NmrA is unlikely to be an active dehydrogenase, however, as the conserved catalytic tyrosine in SDRs is absent in NmrA, and thus the nucleotide binding to NmrA could have a regulatory function. ...”

NMR studies on 2-oxoglutarate oxygenases за авторством Leung, IKH

“...The work included enzyme mechanistic studies, NMR method development, protein NMR and method development for inhibitor discovery....”

Post-translational mutagenesis for installation of natural and unnatural amino acid side chains into recombinant proteins за авторством Wright, T, Davis, B

“...Furthermore, as the side chains are constructed chemically, many unnatural modifications can also be directly introduced as part of the side chain, including isotope reporters (19F, 13C) that can be used in biophysical experiments such as protein NMR. From a suitable cysteine mutant of the target protein, the entire procedure for this chemical post-translational mutation takes 2 d and is readily performed by nonchemists....”

Covalent penicillin-protein conjugates elicit anti-drug antibodies that are clonally and functionally restricted за авторством Deimel, LP, Moynié, L, Sun, G, Lewis, V, Turner, A, Buchanan, CJ, Burnap, SA, Kutuzov, M, Kobras, CM, Demyaneko, Y, Mohammed, S, Stracy, M, Struwe, WB, Baldwin, AJ, Naismith, J, Davis, BG, Sattentau, QJ

“...Deep B cell clonotyping reveals a dominant murine clonal antibody class encompassing phylogenetically-related IGHV1, IGHV5 and IGHV10 subgroup gene segments. Protein NMR and x-ray structural analyses reveal that these drive structurally convergent binding modes in adduct-specific antibody clones. ...”

Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR за авторством Rowbotham, JS, Nicholson, JH, Ramirez, MA, Urata, K, Todd, PMT, Karunanithy, G, Lauterbach, L, Reeve, HA, Baldwin, AJ, Vincent, KA

“...To demonstrate the benefits of the approach for enabling the workflow of protein NMR chemists, we prepared&nbsp;<small>L</small>-[&alpha;-<small>²</small>H,<small>¹⁵</small>N, &beta;-<small>¹³</small>C]-alanine and integrated it into a large (&gt;400 kDa) heat-shock protein oligomer, which was subsequently analysable by methyl-TROSY techniques, revealing new structural information....”

Self-assembly of a barnacle cement protein (MrCP20) into adhesive nanofibrils with concomitant regulation of CaCO₃ polymorphism за авторством Mohanram, Harini, Georges, Tristan, Pervushin, Konstantin, Azaïs, Thierry, Miserez, Ali

“...Simultaneously, AFM and TEM investigations show that MrCP20 undergoes fibrillization triggered by a pH drift arising during CaCO3 mineralization, leading to amyloid-like nanofibrils. Based on protein NMR, this mechanism appears to be stabilized by the reduction of intramolecular disulfide bonds. ...”
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Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria за авторством Schmidt-Rohr, Klaus, Fritzsching, Keith J., Hong, Mei

“...The refined chemical shift distributions are utilized in a simple quality test (SQAT) that should be applied to new protein NMR data before deposition in a databank, and they could benefit many other chemical-shift based tools....”
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The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins за авторством Phillips, Margaret

“...Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool used to study both the structure and dynamics of proteins. NMR can be used for studying both crystal-like and intrinsically disordered proteins. ...”
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Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded за авторством Liang, Yu, Ye, Hong, Kang, Cong Bao, Yoon, Ho Sup

“...The analysis of the backbone 1H, 13C, and 15N resonances, 3JHNα coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. ...”
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Biochemical and biophysical studies of the prokaryotic proton dependent oligopeptide transporters за авторством Solcan, N

Structural studies of integrin activation за авторством Anthis, N, Nicholas J. Anthis