Biochemists simulate a protein-folding chaperone's functional dance Phys.Org
A recent advance in understanding of the role of an interdomain linker in Hsp70 chaperones by Gierasch's group at UMass Amherst required clever computational techniques, massive computing power and masterful use of NMR, she says. Credit: UMass ...
UMass Amherst Biochemists Simulate a Protein-Folding Chaperone's Functional Dance - UMass News and Media Relations
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UMass News and Media Relations
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UMass Amherst Biochemists Simulate a Protein-Folding Chaperone's Functional Dance
UMass News and Media Relations
Gierasch says Wenli Meng, a master of nuclear magnetic resonance (NMR) techniques, obtained NMR data that validated the simulations. The linker is just 12 amino acids long, and Meng was able to directly extract linker information from among 636 amino ...
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08-29-2017 05:35 PM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
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Phys.Org
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Light microscopy provides a deep look into protein structure - Phys.org
Phys.Org
Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ...
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01-25-2017 11:13 PM
[NMR paper] Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Related Articles Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Proc Natl Acad Sci U S A. 2016 Jun 13;
Authors: Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C
Abstract
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of...
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06-15-2016 11:12 PM
A DsbA-Deficient Periplasm Enables Functional Display of a Protein with Redox-Sensitive Folding on M13 Phage
A DsbA-Deficient Periplasm Enables Functional Display of a Protein with Redox-Sensitive Folding on M13 Phage
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00392/20160601/images/medium/bi-2016-003924_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00392
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
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Biochemists reveal interaction between tumor suppressor protein and chaperone
News-Medical.net
Using nuclear magnetic resonance (NMR) spectroscopy, the scientists at the Bavarian NMR Center in Garching were able for the first time to characterize the interaction surfaces between Hsp90 and p53 and show that p53 binds to Hsp90 in an already ...
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