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Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix, MiTeGen etc. - Jewish Life News

Protein Crystallography Market 2020 | Worldwide Opportunities, Driving Forces, Future Potential 2026: Hampton Research, Molecular Dimensions, PerkinElmer, GE Healthcare, Danaher, Bruker, Agilent, Hampton Research, Jena Bioscience, Rigaku, Formulatrix, MiTeGen etc. Jewish Life News Read here
0 Replies | 2 Views
(2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast - Cole of Duty
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar (2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast - Cole of Duty

(2020-2025) Protein Crystallization Size, Share, Trends, Growth, Regional Outlook and Forecast Cole of Duty Read here
0 Replies | 3 Views
[NMR paper] Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.

Related Articles Nanoparticle-assisted NMR spectroscopy: A chemosensing perspective.

Prog Nucl Magn Reson Spectrosc. 2020 Apr;117:70-88

Authors: De Biasi F, Mancin F, Rastrelli F

Abstract
Sensing methodologies for the detection of target compounds in mixtures are important in many different contexts, ranging from medical diagnosis to environmental analysis and quality assessment. Ideally, such detection methods should allow for both identification and quantification of the targets, minimizing the possibility of false positives. With very few exceptions, most of the available sensing techniques rely on the selective interaction of the analyte with some detector, which in turn produces a signal as a result of the interaction. This approach hence provides indirect information on the targets, whose identity is generally ensured by comparison with known standards, if available, or by the selectivity of the sensor system itself. Pursuing a different approach, NMR chemosensing aims at generating signals directly from the analytes, in the form of a (complete) NMR spectrum. In this way, not only are the targets unequivocally identified, but it also becomes possible to identify and assign the structures of unknown species. In this review we show how relaxation- and diffusion-based NMR techniques, assisted by appropriate... [Read More]
0 Replies | 6 Views
[NMR paper] A solid-state NMR tool box for the investigation of ATP-fueled protein engines.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar A solid-state NMR tool box for the investigation of ATP-fueled protein engines.

Related Articles A solid-state NMR tool box for the investigation of ATP-fueled protein engines.

Prog Nucl Magn Reson Spectrosc. 2020 Apr;117:1-32

Authors: Wiegand T

Abstract
Motor proteins are involved in a variety of cellular processes. Their main purpose is to convert the chemical energy released during adenosine triphosphate (ATP) hydrolysis into mechanical work. In this review, solid-state Nuclear Magnetic Resonance (NMR) approaches are discussed allowing studies of structures, conformational events and dynamic features of motor proteins during a variety of enzymatic reactions. Solid-state NMR benefits from straightforward sample preparation based on sedimentation of the proteins directly into the Magic-Angle Spinning (MAS) rotor. Protein resonance assignment is the crucial and often time-limiting step in interpreting the wealth of information encoded in the NMR spectra. Herein, potentials, challenges and limitations in resonance assignment for large motor proteins are presented, focussing on both biochemical and spectroscopic approaches. This work highlights NMR tools available to study the action of the motor domain and its coupling to... [Read More]
0 Replies | 4 Views
[NMR paper] NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

Related Articles NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

Biochemistry. 2020 May 29;:

Authors: Zhang N, Liu J, Liu Y, Wu W, Fang J, Da XD, Wang S, Zhang WB

Abstract
The interplay between protein folding and chemical reaction has been an intriguing subject. In this contribution, we report the study of SpyTag and SpyCatcher reactive mutants using combined techniques of SDS-PAGE, LC-MS, circular dichroism, and NMR spectroscopy. It was found that the wild-type SpyCatcher is well-folded in solution and docks with SpyTag to form an intermediate that promotes isopeptide formation. By contrast, the double mutant SpyCatcherVA is disordered in solution, yet remains reactive toward SpyTag, forming a well-folded covalent complex. Control experiments using the catalytically inactive mutants further reveal the critical role of the isopeptide bond in stabilizing the otherwise loose SpyTag-SpyCatcherVA complex, amplifying the effect of minute sequence disparity. We believe that the synergy between protein folding and isopeptide bonding is an effective way to enhance protein stability and engineer protein-protein interactions.


PMID: 32469203... [Read More]
0 Replies | 4 Views
[NMR paper] Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.

Related Articles Molecular motions and interactions in aqueous solutions of thymosin-?4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.

Chemphyschem. 2020 May 29;:

Authors: Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K

Abstract
Wide-line 1 H NMR measurements were extended and all results were interpreted in a thermodynamics* based new approach on aqueous solutions of thymosin-? 4 (T? 4 ), stabilin C-terminal domain (CTD) and their 1:1 complex. Energy distributions of potential barriers controlling the motion of protein-bound water molecules were determined. Heterogeneous and homogeneous regions were found in the protein-water interface. The measure of heterogeneity of this interface gives quantitative value for the portion of disordered parts in the protein. Ordered structural elements were found extending up to ~20% of the individual whole proteins. About 40% of the binding sites of free T? 4 get involved in bonds holding the complex together. The complex has the most heterogeneous solvent accessible surface (SAS) in terms of protein-water interactions. The complex is more disordered than T? 4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.
... [Read More]
0 Replies | 4 Views
[NMR paper] 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16).
May 31, 2020 - 3:53 PM - by nmrlearner
nmrlearner's Avatar 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16).

Related Articles 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16).

Biomol NMR Assign. 2020 May 28;:

Authors: Thapa CJ, Haataja T, Pentikäinen U, Permi P

Abstract
Protein Phosphatase 2A, PP2A, the principal Serine/threonine phosphatase, has major roles in broad range of signaling pathways that include regulation of cell cycle, cell proliferation and neuronal signaling. The loss of function of PP2A is linked with many human diseases, like cancer and neurodegenerative disorders. Protein phosphatase 2A (PP2A) functions as tumor suppressor and its tumor suppressor activity is inhibited by the overexpression of PP2A inhibitor proteins in most of the cancers. ARPP-19/ARPP-16 has been identified as one of the potential PP2A inhibitor proteins. Here, we report the resonance assignment of backbone 1H, 13C and 15N atoms of human ARPP-19 and ARPP-16 proteins. These chemical shift values can provide valuable information for the further study of the dynamics and interaction of ARPP-proteins to PP2A using NMR spectroscopy.


PMID: 32468417 [PubMed - as supplied by publisher]



... [Read More]
0 Replies | 4 Views
[ssNMR] Post-doc position in the Nieuwkoop Lab
May 29, 2020 - 4:59 PM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[ssNMR] Post-doc position in the Nieuwkoop Lab



The Nieuwkoop lab seeks a post-doctoral researcher to help start a project on the structural biology of the PTEN protein. We use fast spinning solid-state NMR to study protein-lipid interactions. In this project, we seek to understand the functional role of PIP binding by the C2 domain of PTEN. The PTEN C2 domain will be expressed with isotopic labeling to for backbone and side-chain NMR assignments as nanocrystals and bound to its PIP ligand in liposomes. This project will depend on novel ssNMR experiments, optimized sample preparation, and specialized NMR equipment to assess structural and dynamical changes in the bound and unbound protein.


Contact Andy at an567@chem.rutgers.edu for more details and apply here: http://jobs.rutgers.edu/postings/101163


Go to The DNP-NMR Blog for more info.
0 Replies | 5 Views
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