S
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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Journal ArticleDOI
The radius of gyration of an apomyoglobin folding intermediate.
David Eliezer,Patricia A. Jennings,Peter E. Wright,Sebastian Doniach,Keith O. Hodgson,Hirotsugu Tsuruta +5 more
TL;DR: Improved improvements in time-resolved small angle x-ray scattering (SAXS) experiments allow direct measurement of the time-dependent change of R{sub g} ofmore » a protein as it folds in the millisecond to second time frame, and initiated studies of the refolding of apoMb using this technique, under conditions similar to those employed in previous work.
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The Fastest Global Events in RNA Folding: Electrostatic Relaxation and Tertiary Collapse of the Tetrahymena Ribozyme ☆
Rhiju Das,Lisa W. Kwok,Ian S. Millett,Yu Bai,Thalia T. Mills,Jaby Jacob,Jaby Jacob,Gregory S. Maskel,Soenke Seifert,Simon G. J. Mochrie,Pappannan Thiyagarajan,Sebastian Doniach,Lois Pollack,Daniel Herschlag +13 more
TL;DR: This paper used X-ray scattering to monitor the fastest global shape changes of the Tetrahymena ribozyme under different ionic conditions and with RNA mutations that remove long-range tertiary contacts.
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Unusual compactness of a polyproline type II structure
Bojan Zagrovic,Jan Lipfert,Eric J. Sorin,Ian S. Millett,Wilfred F. van Gunsteren,Sebastian Doniach,Vijay S. Pande +6 more
TL;DR: A study of a long-range property: the radius of gyration of an alanine-based peptide, Ace-(diaminobutyric acid)2-(Ala)7-(ornithine)2-NH2, which is believed to adopt a PPII fold based on short-range techniques such as NMR and CD.
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Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved.
TL;DR: An elastic network model of polymerases is used and it is hypothesized that the residues that transmit the signal for the open/closed transition are also strongly conserved, and mutations of the mechanical "hot spots" can compromise the efficiency of the enzyme.
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Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates
Vladimir N. Uversky,Anton S. Karnoup,Daniel J. Segel,Sangita Seshadri,Sebastian Doniach,Anthony L. Fink +5 more
TL;DR: In this article, the authors characterized the refolding of acid-unfolded staphylococcal nuclease (SNase) induced by anions, and revealed the existence of three different partially folded intermediates (A states).