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Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deers, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA Volume 109 Issue 13 Pages from 5080 to 5085). This paper studies the molecular structure of rabbit prion protein wild-type and mutants by molecular dynamics techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

The Wild Rabbit, 1891. Félix Bracquemond (French, 1833–1914). Etching; sheet: 33.5 x 48.7 cm (13 3/16 x 19 3/16 in.); platemark: 25 x 34 cm (9 13/16 x 13 3/8 in.). The Cleveland Museum of Art, Gift of Ralph King, the Frederick Keppel Memorial 1920.654

Book digitized by Google from the library of the University of Michigan and uploaded to the Internet Archive by user tpb.

Book digitized by Google from the library of Harvard University and uploaded to the Internet Archive by user tpb.

Book digitized by Google from the library of Harvard University and uploaded to the Internet Archive by user tpb.

29 p. :

Includes bibliographical references (p. 150) and index

Includes bibliographical references (p. 150) and index

Includes bibliographical references (p. 150) and index

Includes bibliographical references (p. 150) and index