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Identifier 000424544
Title Σχέσεις αλληλουχίας - δομής πρωτεϊνών μέσω μελέτης αντίστροφων αλληλουχιών
Alternative Title Investigation of the relationship between sequence and structure in proteins: studies of inverse amino acid sequences
Author Κεφάλα, Αικατερίνη
Thesis advisor Κοκκινίδης, Μιχαήλ
Abstract The 3D structure of a protein is directly connected with its function and for a long time it was believed that a folded structure is a prerequisite for a protein in order to be functional. The last decades though, significant methods have been developed and therefore the folding states of native proteins, folded/structured, unfolded/unstructured, molten globule and intrinsically disordered, have been determined and characterized. The four different protein folding states are determinant for the protein molecules function. The information about how a polypeptide chain will fold is encoded by its amino acid sequence. The genetic code is characterized by specific rules, according to which we get the polypeptide chain, whereas the code that connects the protein folding with its sequence is far more complicated. Considering the remarkable relation between protein structure and function, it is important to understand the rules that determine the protein folding pathway, as well as the protein folding states. Several research studies investigate the protein folding problem and the relationship between amino acid sequence and structure through limited extend or point mutations. In this study, the main goal is to approach this problem in an extreme way, through inverting the amino acid sequence. In this way we investigate how dissimilar two sequences can be and still adopt the same fold, as well as the folding states of these unnatural sequences. The tool for investigating the above topics is Rop protein. Rop forms one of the most common and simple structural motifs, the 4-α-helical bundle. Based on the wild type Rop and one of its mutants, RM6, the reverse sequences rRop and rRM6, have been designed and studied. Using biophysical and structural methods, such as size exclusion chromatography, circular dichroism, small angle X-ray scattering and X-ray crystallography, we studied the characteristics of the folding pathway of the reverse molecules and we compared their folding states with the forward ones. In addition, we observed the formation of hydrogel from the rRM6 molecule, which is a promising biomaterial for potential biological applications.
Language Greek
Subject Protein folding
Reverse sequences
Αναδίπλωση πρωτεϊνών
Αντίστροφες αλληλουχίες
Issue date 2019-11-29
Collection   Faculty/Department--Faculty of Sciences and Engineering--Department of Biology--Doctoral theses
  Type of Work--Doctoral theses
Permanent Link https://elocus.lib.uoc.gr//dlib/5/6/0/metadata-dlib-1567786040-241724-5127.tkl Bookmark and Share
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