Alzheimer's protein structure suggests new treatment directions Eureka! Science News
The Vanderbilt researchers used nuclear magnetic resonance and electron paragmagnetic resonance spectroscopy to determine the structure of C99, which has one membrane-spanning region. They were surprised to discover what appeared to be a "binding" ...
Alzheimer's protein structure suggests new treatment directions - Eureka! Science News More...
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A new tool to reveal structure of proteins - Eureka! Science News
A new tool to reveal structure of proteins - Eureka! Science News
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A new tool to reveal structure of proteins
Eureka! Science News
For roughly a decade, a technique called solid state nuclear magnetic resonance (NMR) spectroscopy has allowed researchers to detect the arrangements of atoms in proteins that defy study by traditional laboratory tools such as X-ray crystallography.
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03-19-2012 10:30 PM
A chaperone system guides tail-anchored membrane proteins to their destined ... - Eureka! Science News
A chaperone system guides tail-anchored membrane proteins to their destined ... - Eureka! Science News
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Eureka! Science News
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A chaperone system guides tail-anchored membrane proteins to their destined ...
Eureka! Science News
... methods such as X-Ray Crystallography and NMR-Spectroscopy as well as biochemical and cell-biological approaches. In detailed biophysical studies Volker Dötsch´s research group showed that the central cha-peron of the responsible protein complex, ...
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[NMR paper] NMR study suggests a major role for Arg111 in maintaining the structure and dynamical
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Related Articles NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M)...
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11-17-2010 11:15 PM
[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...