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"Scaling
Behavior and Structure of Denatured Proteins." Ding F, Jha RK,
and Dokholyan NV. 2005 Structure Jul;13(7):1047-54. Cover
caption:
Folded and unfolded states of a lily. An ensemble of random coil conformations
with no persistent local and global structures has long been accepted
as the classical model of denatured proteins due to its consistency
with the experimentally determined scaling of protein sizes. However,
recent
NMR spectroscopy studies on proteins at high chemical denaturant concentrations
suggest the presence of significant amounts of native-like structures,
in contrast to the classical random coil picture of denatured proteins.
The reconciliation of these seemingly opposing observations is described
by Ding et al. (cited above). Denatured states (depicted by the unfolded
lily) indeed have strong local conformational bias toward native states
(depicted by the folded lily), while a random coil power law scaling
of protein sizes is preserved.
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"Molecular
Origin of Polyglutamine Aggregation in Neurodegenerative Diseases." Sagar
D. Khare, Feng Ding, Kenneth N. Gwanmesia, and Nikolay V. Dokholyan. PLoS
Comp Biol 1(3):e30.
Cover
caption:
The image depicts a rendering of a ß-helix
structure formed by a polyglutamine peptide, putatively implicated
in numerous protein–aggregation diseases. The merged image of
the eye, the polyglutamine structure, and the simulation program code
represents the ability to capture aggregation-prone protein conformations
using computer simulations.
For more information on the Dokholyan lab:
Dokholyan lab website
Dokholyan CCGS webpage |
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