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Random-coil behavior and the dimensions of chemically unfolded proteins.
It appears that the mean dimensions of the large majority of chemically denatured proteins are effectively indistinguishable from themean dimensions of a random-coil ensemble.
Biophysical Properties of the Synucleins and Their Propensities to Fibrillate
It is shown that, although they have similar biophysical properties to α- Synuclein, β- And γ-synucleins inhibit α-syn DNA fibril formation and a model for the inhibition is proposed.
Quantitative and comprehensive decomposition of the ion atmosphere around nucleic acids.
The first complete accounting of the ion atmosphere is provided, using buffer equilibration and atomic emission spectroscopy (BE-AES) to accurately quantitate the cation association and anion depletion and to parse the electrostatic contribution from the overall thermodynamics of important biological processes.
Changes in biomolecular conformation seen by small angle X-ray scattering.
- S. Doniach
- ChemistryChemical reviews
- 25 April 2001
Relation Between Obesity and Blunted Striatal Response to Food Is Moderated by TaqIA A1 Allele
Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins.
Long single α-helical tail domains bridge the gap between structure and function of myosin VI
- B. Spink, S. Sivaramakrishnan, J. Lipfert, S. Doniach, J. Spudich
- Biology, ChemistryNature Structural &Molecular Biology
- 30 May 2008
It is demonstrated that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single α-helix of ∼10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail.
Size and shape of detergent micelles determined by small-angle X-ray scattering.
- J. Lipfert, L. Columbus, Vincent B. Chu, S. Lesley, S. Doniach
- Chemistry, BiologyThe journal of physical chemistry. B
- 9 October 2007
Combined, these data provide a comprehensive view of the determinants of micelle formation and serve as a starting point to correlate detergent properties with detergent-protein interactions.
Partially folded intermediates in insulin fibrillation.
- Atta Ahmad, I. Millett, S. Doniach, V. Uversky, A. Fink
- Chemistry, BiologyBiochemistry
- 10 September 2003
The data suggest that under physiological conditions, the fibrillation of insulin involves both changes in the association state (with rate-limiting hexamer dissociation) and conformational changes, leading to formation of the amyloidogenic expanded monomer intermediate.