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Sebastian Doniach

Researcher at Stanford University

Publications -  217
Citations -  20947

Sebastian Doniach is an academic researcher from Stanford University. The author has contributed to research in topics: Small-angle X-ray scattering & Scattering. The author has an hindex of 78, co-authored 217 publications receiving 19797 citations. Previous affiliations of Sebastian Doniach include Genomics Institute of the Novartis Research Foundation & Cornell University.

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Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin.

Sergei E. Permyakov, +5 more
- 01 Dec 2003 - 
TL;DR: It is shown here that CaD136 does not have globular structure, has low secondary structure content, is essentially noncompact, and is characterized by the absence of distinct heat absorption peaks, i.e. it belongs to the family of natively unfolded (or intrinsically unstructured) proteins.
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Dynamic charge interactions create surprising rigidity in the ER/K α-helical protein motif

Sivaraj Sivaramakrishnan, +4 more
- 09 Sep 2008 - 
TL;DR: The significant rigidity of the ER/K α-helix can help regulate protein function, as a force transducer between protein subdomains, making it a promising tool in designing synthetic proteins.
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Association-induced folding of globular proteins

Vladimir N. Uversky, +3 more
- 12 May 1998 - 
TL;DR: It is shown that under some conditions the association of partially folded intermediates can induce additional structure leading to soluble aggregates with many native-like properties, including those of staphylococcal nuclease.
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Monte Carlo simulation of flux lattice melting in a model high-Tc superconductor.

Seunghwa Ryu, +7 more
- 03 Feb 1992 - 
TL;DR: It is observed that the transition temperature shifts downward toward the two-dimensional melting limit as the density of flux lines increases, and a significant difference in shear modulus is observed when flux cutting or reconnection is allowed.
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Evidence of an associative intermediate on the myoglobin refolding pathway.

David Eliezer, +5 more
- 01 Aug 1993 - 
TL;DR: Time-resolved small-angle x-ray scattering using the stopped-flow method has been applied successfully to investigate the refolding of myoglobin and shows a decrease in amplitude which is clearly not engendered by the compaction of the protein, but does correspond well to a dimer dissociation process.