alexa Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon Sequences | OMICS International
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
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Research Article

Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon Sequences

Banach M1, Kalinowska B1,2, Konieczny L3 and Roterman I1*

1Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Łazarza 16, 31-530 Krakow, Poland

2Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Łojasiewicza 8, 30-348 Krakow, Poland

3Chair of Medical Biochemistry, Jagiellonian University Medical College, Kopernika 7, 31-034 Krakow, Poland

*Corresponding Author:
Irena Roterman
Department of Bioinformatics and Telemedicine
Jagiellonian University Medical College, Łazarza 16
31-530 Krakow, Poland
Tel: 48126199693
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.

Abstract

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.

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