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An NMR and molecular dynamics investigation of the avian prion hexarepeat conformational features in solution
- Source :
-
Chemical Physics Letters . Jul2007, Vol. 442 Issue 1-3, p110-118. 9p. - Publication Year :
- 2007
-
Abstract
- Abstract: The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and molecular dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions. [Copyright &y& Elsevier]
- Subjects :
- *MOLECULAR dynamics
*DYNAMICS
*HYDROGEN-ion concentration
*BUFFER solutions
Subjects
Details
- Language :
- English
- ISSN :
- 00092614
- Volume :
- 442
- Issue :
- 1-3
- Database :
- Academic Search Index
- Journal :
- Chemical Physics Letters
- Publication Type :
- Academic Journal
- Accession number :
- 25491729
- Full Text :
- https://doi.org/10.1016/j.cplett.2007.05.046