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
Effects of nitration on the structure and aggregation of α-synuclein
Vladimir N. Uversky,Ghiam Yamin,Larissa A. Munishkina,Mikhail A. Karymov,Ian S. Millett,Sebastian Doniach,Yuri L. Lyubchenko,Anthony L. Fink +7 more
TL;DR: The properties of nitrated α-synuclein were investigated using a variety of biophysical and biochemical techniques and revealed that nitration led to formation of a partially folded conformation with increased secondary structure relative to the intrinsically disordered structure of the monomer, and to oligomerization at neutral pH.
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Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
Daniel J. Segel,Annett Bachmann,James Hofrichter,Keith O. Hodgson,Sebastian Doniach,Thomas Kiefhaber +5 more
TL;DR: In this paper, the authors used synchrotron radiation, together with continuous flow and mixing techniques to monitor refolding of lysozyme at pH 5.2 and showed that a major chain collapse occurs in the dead-time of mixing.
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A Lysozyme Folding Intermediate Revealed by Solution X-ray Scattering
TL;DR: Simplified partially folded models, based on the crystal structure of hen lysozyme, support a working model for the intermediate, whose structure may be correlated with that of the kinetic intermediate found in the refolding pathway studied by Dobson and coworkers.
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Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH.
Vladimir N. Uversky,Joel R. Gillespie,Ian S. Millett,Anna V. Khodyakova,Anatoly M. Vasiliev,Tatyana V. Chernovskaya,Raisa N. Vasilenko,Galina D. Kozlovskaya,Dmitry A. Dolgikh,Anthony L. Fink,Sebastian Doniach,Vyacheslav M. Abramov +11 more
TL;DR: Interestingly, prothymosin α underwent a cooperative transition from the unfolded state into a partially folded conformation on lowering the pH, and it is possible that such conformational changes may be associated with the protein function.
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Evaluation of ion binding to DNA duplexes using a size-modified Poisson-Boltzmann theory.
TL;DR: An existing size-modified Poisson-Boltzmann (SMPB) theory is generalized and a new numerical implementation that solves the generalized theory around complex, atomistic representations of biological molecules is developed, demonstrating that the theory is predictive.