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Protein dynamics play major role in directed evolution's success - Chemical & Engineering News
Nov 23, 2020 - 7:11 PM - by nmrlearner
nmrlearner's Avatar Protein dynamics play major role in directed evolution's success Chemical & Engineering News
Protein dynamics play major role in directed evolution's success - Chemical & Engineering News
More...
0 Replies | 3 Views
(1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 - DocWire News
Nov 22, 2020 - 9:18 PM - by nmrlearner
nmrlearner's Avatar (1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 - DocWire News

(1)H, (13)C, and (15)N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7 DocWire News Read here
0 Replies | 7 Views
Structure of SARS-CoV-2 envelope protein solved by NMR - Chemical & Engineering News
Nov 22, 2020 - 4:05 AM - by nmrlearner
nmrlearner's Avatar Structure of SARS-CoV-2 envelope protein solved by NMR - Chemical & Engineering News

Structure of SARS-CoV-2 envelope protein solved by NMR Chemical & Engineering News Read here
0 Replies | 8 Views
Discovery of pH-dependent 'switch' in interaction between pair of protein molecules - Science Codex
Nov 22, 2020 - 4:05 AM - by nmrlearner
nmrlearner's Avatar Discovery of pH-dependent 'switch' in interaction between pair of protein molecules Science Codex
Discovery of pH-dependent 'switch' in interaction between pair of protein molecules - Science Codex
More...
0 Replies | 7 Views
[NMR paper] An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.
Nov 22, 2020 - 4:05 AM - by nmrlearner
nmrlearner's Avatar An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.

Related Articles An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.

Proteins. 2020 01;88(1):82-93

Authors: Turupcu A, Bowen AM, Di Paolo A, Matagne A, Oostenbrink C, Redfield C, Smith LJ

Abstract
The X-ray structure of lysozyme from bacteriophage lambda (? lysozyme) in complex with the inhibitor hexa-N-acetylchitohexaose (NAG6) (PDB: 3D3D) has been reported previously showing sugar units from two molecules of NAG6 bound in the active site. One NAG6 is bound with four sugar units in the ABCD sites and the other with two sugar units in the E'F' sites potentially representing the cleavage reaction products; each NAG6 cross links two neighboring ? lysozyme molecules. Here we use NMR and MD... [Read More]
0 Replies | 22 Views
Evolutionary dynamics of SARS-CoV-2 nucleocapsid protein and its consequences - Wiley
Nov 21, 2020 - 8:41 AM - by nmrlearner
nmrlearner's Avatar Evolutionary dynamics of SARS-CoV-2 nucleocapsid protein and its consequences - Wiley

Evolutionary dynamics of SARS-CoV-2 nucleocapsid protein and its consequences Wiley Read here
0 Replies | 11 Views
[NMR paper] Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.
Nov 21, 2020 - 8:41 AM - by nmrlearner
nmrlearner's Avatar Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.

Related Articles Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.

IUCrJ. 2020 Nov 01;7(Pt 6):1019-1027

Authors: Lee K, Yeo KJ, Choi SH, Lee EH, Kim BK, Kim S, Cheong HK, Lee WK, Kim HY, Hwang E, Woo JR, Lee SJ, Hwang KY

Abstract
Protein dimerization or oligomerization resulting from swapping part of the protein between neighboring polypeptide chains is known to play a key role in the regulation of protein function... [Read More]
0 Replies | 18 Views
[NMR paper] Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.
Nov 21, 2020 - 8:41 AM - by nmrlearner
nmrlearner's Avatar Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.

Related Articles Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.

Sci Rep. 2020 Nov 18;10(1):20069

Authors: Wu N, Kobayashi N, Tsuda K, Unzai S, Saotome T, Kuroda Y, Yamazaki T

Abstract
Gaussia luciferase (GLuc) is a small luciferase (18.2*kDa; 168 residues) and is thus attracting much attention as a reporter protein, but the lack of structural information is hampering further application. Here, we report the first solution structure of a fully active, recombinant GLuc determined by heteronuclear multidimensional NMR. We obtained a natively folded GLuc by bacterial expression and efficient refolding using a Solubility Enhancement Petide (SEP)*tag. Almost perfect assignments of GLuc's 1H, 13C and 15N backbone signals were obtained. GLuc structure was determined using CYANA, which automatically identified over 2500 NOEs of... [Read More]
0 Replies | 11 Views
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