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 Protein Crystallization Market 2020: Potential growth, attractive valuation make it is a long-term investment | Know the COVID19 Impact | Top Players: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, etc. | InForGrowth - T |
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Aug 26, 2020 - 2:46 PM - by nmrlearner
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Protein Crystallization Market 2020: Potential growth, attractive valuation make it is a long-term investment | Know the COVID19 Impact | Top Players: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, etc. | InForGrowth - The Scarlet
Protein Crystallization Market 2020: Potential growth, attractive valuation make it is a long-term investment | Know the COVID19 Impact | Top Players: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, etc. | InForGrowth The Scarlet Read here
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0 Replies | 18 Views
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[NMR paper] Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET. |
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Aug 26, 2020 - 2:46 PM - by nmrlearner
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Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Related Articles Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
J Am Chem Soc. 2020 Aug 25;:
Authors: Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC
Abstract
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging, but of great interest, since their conformational ensembles are the link between their sequences and functions. An accurate description of IDP conformational ensembles depends crucially on the amount and quality of the experimental data, how it is integrated, and if it mutually supports a consistent structural picture. We used integrative modelling and validation to apply conformational restraints and assess agreement with the most common structural techniques for IDPs: Nuclear Magnetic Resonance (NMR) spectroscopy, Small-angle X-ray Scattering (SAXS), and single-molecule Förster Resonance Energy Transfer (smFRET) reach concordance on structural ensembles for Sic1 and phosphorylated Sic1 (pSic1). To resolve apparent discrepancies between smFRET and SAXS, we integrated SAXS data with non-smFRET (NMR) data and reserved the new smFRET data for Sic1 and pSic1, as an... [Read More]
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0 Replies | 13 Views
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[NMR paper] Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics. |
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Aug 25, 2020 - 1:19 PM - by nmrlearner
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Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
Related Articles Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
Biochim Biophys Acta Biomembr. 2020 Aug 21;:183451
Authors: Hu W, Bhattacharya S, Hong T, Wong P, Li L, Vaidehi N, Kalkum M, Shively JE
Abstract
AIIt, a heterotetramer of S100A10 (P11) and Annexin A2, plays a key role in calcium dependent, membrane associations with a variety of proteins. We previously showed that AIIt interacts with the short cytoplasmic domain (12 amino acids) of CEACAM1 (CEACAM1-SF). Since the cytoplasmic domains of CEACAM1 help regulate the formation of cis- or trans-dimers at the cell membrane, we investigated the possible role of their association with AIIt in this process. Using NMR and molecular dynamics, we show that AIIt and its pseudoheterodimer interacts with two molecules of short cytoplasmic domain isoform peptides, and that interaction depends on the binding motif 454-Phe-Gly-Lys-Thr-457 where Phe-454 binds in a hydrophobic pocket of AIIt, the null mutation Phe454Ala reduces binding by 2.5 fold, and the pseudophosphorylation mutant Thr457Glu reduces binding by three fold. Since these two... [Read More]
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0 Replies | 25 Views
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[NMR paper] Solution structure of insect CSP and OBPs by NMR. |
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Aug 24, 2020 - 9:54 PM - by nmrlearner
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Solution structure of insect CSP and OBPs by NMR.
Solution structure of insect CSP and OBPs by NMR.
Methods Enzymol. 2020;642:169-192
Authors: Leone S, Emendato A, Spadaccini R, Picone D
Abstract
Insect odorant binding proteins (OBPs) and chemosensory proteins (CSPs) are proteins deputed to the solubilization, transport and stabilization of lipophilic and odorant compounds. These proteins have a conserved fold, which undergoes massive structural rearrangements in order to accommodate medium to large-sized lipophilic ligands. Solution NMR spectroscopy, due to its intrinsically dynamic nature, is the perfect technique to extrapolate structural information and dynamic parameters and to elucidate the conformational changes that occur upon ligand binding. This chapter will describe in detail the experimental protocols for the production and purification of isotope-labeled recombinant CSPs and OBPs for NMR studies. Detailed procedures for spectra acquisition, processing and analysis will be presented, focusing on the protein CSP-sg4 from Schistocerca gregaria as a model. Finally, experiments aimed at providing information on protein flexibility and ligand binding modes will also be described.
PMID: 32828252 [PubMed - as supplied by publisher]
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0 Replies | 25 Views
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