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Title:

The induction of ?-helical structure in partially unfolded HypF-N does not affect its aggregation propensity.

Document type:
Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Ahmad, B; Vigliotta, I; Tatini, F; Campioni, S; Mannini, B; Winkelmann, J; Tiribilli, B; Chiti, F
Abstract:
The conversion of proteins into structured fibrillar aggregates is a central problem in protein chemistry, biotechnology, biology and medicine. It is generally accepted that aggregation takes place from partially structured states of proteins. However, the role of the residual structure present in such conformational states is not yet understood. In particular, it is not yet clear as to whether the ?-helical structure represents a productive or counteracting structural element for protein aggreg...     »
Journal title abbreviation:
Protein Eng Des Sel
Year:
2011
Journal volume:
24
Journal issue:
7
Pages contribution:
553-63
Language:
eng
Fulltext / DOI:
doi:10.1093/protein/gzr018
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/21518735
Print-ISSN:
1741-0126
TUM Institution:
Neurologische Klinik und Poliklinik
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