Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon SequencesBanach M1, Kalinowska B1,2, Konieczny L3 and Roterman I1*
- *Corresponding Author:
- Irena Roterman
Department of Bioinformatics and Telemedicine
Jagiellonian University Medical College, Łazarza 16
31-530 Krakow, Poland
E-mail: [email protected]
Received date: October 14, 2016; Accepted date: November 07, 2016; Published date: November 11, 2016
Citation: Banach M, Kalinowska B, Konieczny L, Roterman I (2016) Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon Sequences. J Proteomics Bioinform 9:264-275. doi: 10.4172/jpb.1000415
Copyright: © 2016 Banach M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The existence of polypeptide chain fragments in which identical sequences translate into different secondary folds gives rise to questions concerning the structural variability associated with amyloidogenesis. In this paper the structural contribution of identical sequences to a common hydrophobic core is assessed on the basis of the fuzzy oil drop model. The model compares the observed hydrophobicity density distribution in a protein molecule to its idealized counterpart, where all hydrophilic residues are exposed on the surface while all hydrophobic residues are internalized. The conformational variability of such fragments is thought to be associated with their role: they either participate in the formation of a stable core, or become involved in mediating the protein’s biological function. The fuzzy oil drop model provides clues as to the role of chameleon sequences in prions, seen as potential loci of conformational changes resulting in amyloidogenesis.