Results 41 to 50 of about 6,813,928 (408)
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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Kinetics and Thermodynamics of Membrane Protein Folding [PDF]
Biomolecules 2014, 4(1), 354-373, 2014 Understanding protein folding has been one of the great challenges in biochemistry and molecular biophysics. Over the past 50 years, many thermodynamic and kinetic studies have been performed addressing the stability of globular proteins. In comparison, advances in the membrane protein folding field lag far behind. Although membrane proteins constitute
arxiv +1 more source
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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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
doaj +1 more source
The impact of hydrodynamic interactions on protein folding rates depends on temperature [PDF]
Phys. Rev. E 97, 032402 (2018), 2017 We investigated the impact of hydrodynamic interactions (HI) on protein folding using a coarse-grained model. The extent of the impact of hydrodynamic interactions, whether it accelerates, retards, or has no effect on protein folding, has been controversial.
arxiv +1 more source
Cold Spring Harbor Perspectives in Biology, 2019 Most of the secreted and plasma membrane proteins are synthesized on membrane-bound ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident chaperones and foldases that assist in their folding and maturation.
G. E. Karagöz +2 more
semanticscholar +1 more source
Chaos of protein folding [PDF]
The 2011 International Joint Conference on Neural Networks, 2011 As protein folding is a NP-complete problem, artificial intelligence tools like neural networks and genetic algorithms are used to attempt to predict the 3D shape of an amino acids sequence. Underlying these attempts, it is supposed that this folding process is predictable.
Bahi, Jacques +2 more
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The kinetics of folding of the NSH2 domain from p85 [PDF]
, 2019 SH2 domains are protein domains that mediate protein-protein interaction through the recognition and binding of specific sequences containing phosphorylated tyrosines.
Gianni, Stefano +3 more
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Protein Folding by Interaction [PDF]
Structure, 2014 Repeat proteins consisting of helical segments seem to fold by a matrix-assisted mechanism in which folded segments induce structure in intrinsically disordered parts of the protein, as shown by Watson and colleagues in this issue of Structure for an Armadillo repeat protein and previously by the Balbach group for an Ankyrin repeat protein.
Johannes Buchner +2 more
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Are protein folds atypical? [PDF]
Proceedings of the National Academy of Sciences, 1998 Protein structures are a very special class among all possible structures. It has been suggested that a “designability principle” plays a crucial role in nature’s selection of protein sequences and structures. Here, we provide a theoretical base for such a selection principle, using a simple model of protein folding based on hydrophobic interactions. A
Hao Li, Ned S. Wingreen, Chao Tang
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