Doğal düzensiz proteinlerin arayüzleri

Until quite recently, the common belief was that every protein has stable tertiary structure. However, now it is widely known that some proteins or regions of the proteins can be unfolded under physiological conditions. The proteins that carry these properties are called as intrinsically disordered proteins or natively unfolded proteins. Disordered proteins play a key role in many critical biological functions. Especially for signalling and regulation, intrinsically disordered proteins are of crucial importance.This project mainly focuses on the differences between ordered and disordered proteins and their interfaces. For this purpose, we separate the proteins in our database into two groups: (1) Disordered, (2) Ordered proteins. We do the analysis according to their structure and chemical nature. Concerning the structural comparison, the accessible surface areas and per residue areas are typical features that we use. Also, we investigate the change of hot spot residues with respect to disorder changes. For comparing the chemical nature, the ratio of the polar amino acids to non-polar amino acids in proteins and interfaces are calculated. Since low hydrophobic content is an important indicator for disordered proteins, polar/apolar ratios are used for comparing hydrophobicity. In addition, binding preferences of intrinsically disordered proteins are analyzed.Also, another aim of this work is to create new interface type for disordered proteins. Interfaces separated into three groups according to their structures and functions. These groups are called as Type 1, Type 2 and Type 3. Thus, our aim is forming Type 4 for disordered proteins.