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Akademický článek
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Autor:
Mina J. Bissell, Rohit V. Pappu, Nicholas Lyle, Jieya Shao, Shirong Cai, CJ Carey, Helen Piwnica-Worms, Marc I. Diamond, S. Joshua Swamidass, Aaron Boudreau
Publikováno v:
Journal of Biological Chemistry. 290:9075-9086
The actin-binding protein profilin-1 (Pfn1) inhibits tumor growth and yet is also required for cell proliferation and survival, an apparent paradox. We previously identified Ser-137 of Pfn1 as a phosphorylation site within the poly-l-proline (PLP) bi
Publikováno v:
Journal of the American Chemical Society. 137:2984-2995
In aqueous solutions with high concentrations of chemical denaturants such as urea and guanidinium chloride (GdmCl) proteins expand to populate heterogeneous conformational ensembles. These denaturing environments are thought to be good solvents for
Publikováno v:
Journal of Chemical Theory and Computation
There is growing interest in the topic of intrinsically disordered proteins (IDPs). Atomistic Metropolis Monte Carlo (MMC) simulations based on novel implicit solvation models have yielded useful insights regarding sequence-ensemble relationships for
Publikováno v:
Biochemistry. 52:2662-2671
The denatured state ensemble (DSE) represents the starting state for protein folding and the reference state for protein stability studies. Residual structure in the DSE influences the kinetics of protein folding, the propensity to aggregate, and pro
Publikováno v:
Biochemical Journal. 449:307-318
Emil Fischer proposed that enzyme specificity could be explained by shape complementarity [1, 2]. He used the metaphor of a lock and key to illustrate how the three-dimensional arrangements of atoms comprising an enzyme and its substrate could enable
Autor:
Oliver D. King, Bonnie Berger, Randal Halfmann, Nicholas Lyle, Rohit V. Pappu, Rajaraman Krishnan, Susan Lindquist, Simon Alberti, Charles W. O'Donnell
Publikováno v:
Molecular Cell. 43(1):72-84
Sequences rich in glutamine (Q) and asparagine (N) residues often fail to fold at the monomer level. This, coupled to their unusual hydrogen-bonding abilities, provides the driving force to switch between disordered monomers and amyloids. Such transi
Publikováno v:
Biophysical Journal. 106(2)
The mechanistic details of protein denaturation are relevant for understanding the nature of the collapse transition that is induced by dilution from denaturing to predominantly aqueous solutions. Concentrated solutions of urea and GdnCl are thought
Publikováno v:
The Journal of chemical physics. 139(12)
Conformational heterogeneity is a defining characteristic of proteins. Intrinsically disordered proteins (IDPs) and denatured state ensembles are extreme manifestations of this heterogeneity. Inferences regarding globule versus coil formation can be
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 110, iss 6
The sizes of unfolded proteins under highly denaturing conditions scale as N 0.59 with chain length. This suggests that denaturing conditions mimic good solvents, whereby the preference for favorable chain–solvent interactions causes intrachain int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa44d7ca45416dc2af3dc2476ea73a5b
https://europepmc.org/articles/PMC3568295/
https://europepmc.org/articles/PMC3568295/