Paper Citing NAMD - Abstract
Krol, M.; Konieczny, L.; Stapor, K.; Wisniowski, Z.; Ziajka, W.; Szoniec, G.; Roterman-Konieczna, I.
Misfolded proteins
PROTEIN FOLDING IN SILICO: PROTEIN FOLDING VERSUS PROTEIN STRUCTURE PREDICTION, Issue 22, 141-164, 2012
Structural analysis of properly folded proteins provides insight into their folding process and the origins of their biological properties; however, an equally rich trove of information presents itself in the form of misfolded proteins, particularly amyloidogenic ones. Such proteins exhibit structural modifications that induce the formation of large-scale fibrillary aggregates. Changes that promote amyloidogenesis also destroy the protein's intended biological activity. Relating the phenomenon of amyloid generation to the proposed folding model suggests the importance of F-type motifs, emerging as a result of structural forms introduced by external forces.
