Results 31 to 40 of about 6,845,089 (390)
Journal of Cellular and Molecular Medicine, 2003 AbstractThe problem of protein folding is that how proteins acquire their native unique three‐dimensional structure in the physiological milieu. To solve the problem, the following key questions should be answered: do proteins fold co‐ or post‐translationally, i.e.
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Progress in Nuclear Magnetic Resonance Spectroscopy, 2017 Protein folding is a highly complex process proceeding through a number of disordered and partially folded nonnative states with various degrees of structural organization. These transiently and sparsely populated species on the protein folding energy landscape play crucial roles in driving folding toward the native conformation, yet some of these ...
Anastasia Zhuravleva, Dmitry M. Korzhnev
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Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
EMBO Molecular Medicine, 2015 The cellular prion protein (PrPC) comprises a natively unstructured N‐terminal domain, including a metal‐binding octarepeat region (OR) and a linker, followed by a C‐terminal domain that misfolds to form PrPSc in Creutzfeldt‐Jakob disease.
Agnes Lau +19 more
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Movement of Chronic Wasting Disease Prions in Prairie, Boreal and Alpine Soils
Pathogens, 2023 Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy negatively impacting cervids on three continents. Soil can serve as a reservoir for horizontal transmission of CWD by interaction with the infectious prion protein (PrPCWD) shed ...
Alsu Kuznetsova +4 more
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Identifying the protein folding nucleus using molecular dynamics [PDF]
, 2000 Molecular dynamics simulations of folding in an off-lattice protein model reveal a nucleation scenario, in which a few well-defined contacts are formed with high probability in the transition state ensemble of conformations.
Buldyrev, Sergey V. +3 more
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Bulletin of the Australian Mathematical Society, 1985 zbMATH Open Web Interface contents unavailable due to conflicting licenses.
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Protein folding disorders: Toward a basic biological paradigm [PDF]
, 2010 Mechanistic 'physics' models of protein folding fail to account for the observed spectrum of protein folding and aggregation disorders, suggesting that a more appropriately biological paradigm will be needed for understanding the etiology ...
Rodrick Wallace
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Protein folds and functions [PDF]
Structure, 1998 The recent rapid increase in the number of available three-dimensional protein structures has further highlighted the necessity to understand the relationship between biological function and structure. Using structural classification schemes such as SCOP, CATH and DALI, it is now possible to explore global relationships between protein fold and ...
Maria Karmirantzou +8 more
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Protein folding rates correlate with heterogeneity of folding mechanism [PDF]
, 2004 By observing trends in the folding kinetics of experimental 2-state proteins at their transition midpoints, and by observing trends in the barrier heights of numerous simulations of coarse grained, C-alpha model, Go proteins, we show that folding rates ...
A. R. Fersht +10 more
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Highly accurate protein structure prediction with AlphaFold
Nature, 2021 Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function. Through an enormous experimental effort1–4, the structures of around 100,000 unique proteins have been determined5, but this ...
J. Jumper +33 more
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