Results 41 to 50 of about 6,845,089 (390)
Are protein folds atypical? [PDF]
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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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
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Protein Folding by Interaction [PDF]
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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Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf+7 more
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PROTEIN FOLDING AND HETEROPOLYMERS [PDF]
57 pages, 7 figures. Uses lprocl.sty (included). To appear in " Spin glasses and random fields ", A.P.
Garel, Thomas+2 more
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Sheep scrapie and deer rabies in England prior to 1800
Eighteenth-century England witnessed the emergence of two neurological diseases in animals. Scrapie, a transmissible spongiform encephalopathy, is a fatal neurodegenerative disease of sheep and goats that appears in classical and atypical forms.
Anthony Ness+2 more
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Simulations of protein folding [PDF]
LATTICE99(Theoretical Developments), 3 pages, latex; new version has better ...
Mark E. Fleharty+2 more
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The Structure of Human Prions: From Biology to Structural Models—Considerations and Pitfalls
The Structure of Human Prions: From Biology to Structural Models — Considerations and ...
Claudia Y. Acevedo-Morantes+1 more
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Prion diseases are fatal, transmissible neurodegenerative disorders whose pathogenesis is driven by the misfolding, self-templating and cell-to-cell spread of the prion protein.
Hailey Pineau, Valerie Sim
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Secondary Forces in Protein Folding.
A complete inventory of the forces governing protein folding is critical for productive protein modeling, including structure prediction and de novo design, as well as understanding protein misfolding diseases of clinical significance.
R. Newberry, Ronald T. Raines
semanticscholar +1 more source