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Technique permits convenient, precise optical imaging of individual proteins - Phys.org
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Technique permits convenient, precise optical imaging of individual proteins - Phys.org

Technique permits convenient, precise optical imaging of individual proteins Phys.org Read here
0 Replies | 1 Views
Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User - Global Forecast to 2025 - Cumulative Impact of COVID-19 - GlobeNewswire
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User - Global Forecast to 2025 - Cumulative Impact of COVID-19 - GlobeNewswire

Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User - Global Forecast to 2025 - Cumulative Impact of COVID-19 GlobeNewswire Read here
0 Replies | 1 Views
Global Protein Crystallization & Crystallography Market Is Expected to Reach USD 1.97 Billion by 2027 : Fior Markets - globenewswire.com
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Global Protein Crystallization & Crystallography Market Is Expected to Reach USD 1.97 Billion by 2027 : Fior Markets - globenewswire.com

Global Protein Crystallization & Crystallography Market Is Expected to Reach USD 1.97 Billion by 2027 : Fior Markets globenewswire.com Read here
0 Replies | 1 Views
Structure of 'immortality protein' now better understood - Science Codex
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Structure of 'immortality protein' now better understood - Science Codex

Structure of 'immortality protein' now better understood Science Codex Read here
0 Replies | 1 Views
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation

ABSTRACT

Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and involved in regulation of biofilm formation in the cyanobacterium Synechococcus elongatus PCC 7942. Se0862 is a class ?+? protein with ???????? topology and roll architecture, consisting of a four-stranded ?-sheet that is flanked by four ?-helices on one side. Conserved surface residues constitute a hydrophobic pocket and charged regions that are likely also present in Se0862 orthologs.

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[NMR paper] Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.

Related Articles Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.

Protein Sci. 2020 Sep 18;:

Authors: Zhang N, Chang YG, Tseng R, Ovchinnikov S, Schwarz R, LiWang A

Abstract
Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and involved in regulation of biofilm formation in the cyanobacterium Synechococcus elongatus PCC 7942. Se0862 is a class ?+? protein with ???????? topology and roll architecture, consisting of a four-stranded ?-sheet that is flanked by four ?-helices on one side.... [Read More]
0 Replies | 1 Views
[NMR paper] Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

Related Articles Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

Proteins. 2020 Sep 18;:

Authors: Fridmanis J, Otikovs M, Brangulis K, T?rs K, Jaudzems K

Abstract
Lyme disease is the most widespread vector-transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five ?-helices and an extended C-terminal loop. The fold is similar to that of Borrelia tunicate outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. This article is protected by copyright. All rights... [Read More]
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[NMR paper] Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.
Sep 21, 2020 - 5:44 PM - by nmrlearner
nmrlearner's Avatar Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.

Related Articles Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.

Biomol NMR Assign. 2020 Sep 18;:

Authors: Pradhan T, Annamalai K, Sarkar R, Hegenbart U, Schönland S, Fändrich M, Reif B

Abstract
The aggregation of antibody light chains is linked to systemic light chain (AL) amyloidosis, a disease where amyloid deposits frequently affect the heart and the kidney. We here investigate fibrils from the ?-III FOR005 light chain (LC), which is derived from an AL-patient with severe cardiac involvement. In FOR005, five residues are mutated with respect to its closest germline gene segment IGLV3-19 and IGLJ3. All mutations are located close to the complementarity determining regions (CDRs). The sequence segments responsible for the fibril formation are not yet known. We use fibrils extracted from the heart of this particular amyloidosis patient as seeds to prepare fibrils for solid-state NMR. We show that the seeds induce... [Read More]
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