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Titel:

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

Dokumenttyp:
Journal Article; Research Support, Non-U.S. Gov't
Autor(en):
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...     »
Zeitschriftentitel:
Protein Eng Des Sel
Jahr:
2011
Band / Volume:
24
Heft / Issue:
7
Seitenangaben Beitrag:
553-63
Sprache:
eng
Volltext / DOI:
doi:10.1093/protein/gzr018
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/21518735
Print-ISSN:
1741-0126
TUM Einrichtung:
Neurologische Klinik und Poliklinik
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