Structural role of exons in hemoglobin

• Autorzy: Piwowar M. , Banach M. , Konieczny L. , Chomilier J. , Roterman I.
• Języki publikacji: EN

Abstrakty

EN

The role of exons can be studied on many levels, one of which pertains to protein structure. It is a well-known fact that secondary structural motifs do not directly correspond to exons: helices, β-sheets and loops have all been identified as encoded by more than one exon. The relation between exon fragments and their involvement in shaping the three-dimensional (3D) structure of a protein body is subject to ongoing studies. In particular, the role of exons in stabilizing tertiary structures can be related to the structure of the hydrophobic core of the protein. Participation of specific polypeptide fragments (single exons) in hydrophobic stabilization reveals the role played by each fragment. In the course of the presented research, exons in selected proteins have been identified on the basis of GenBank files, imported from the nucleotide database at the National Center of Biotechnology Information. Amino acid sequences representing each exon were subsequently traced to parts of 3D structural forms. The participation of each exon fragment in shaping the hydrophobic core of the protein was measured using divergence entropy calculations. It was found that each protein contains at least one exon which encodes a structural fragment in accordance with the theoretical hydrophobic core model. This implies that the likely role of at least one exon in each protein is to generate a hydrophobic core which is, in turn, responsible for tertiary structural stabilization.

Słowa kluczowe

EN

divergence entropy; exons; hemoglobin; hydrophobic core

• Wydawca: Uniwersytet Jagielloński - Collegium Medicum ; Index Copernicus Sp. z o.o.
• Czasopismo: Bio-Algorithms and Med-Systems
• Rocznik: 2013
• Tom: Vol. 9, no. 2
• Strony: 81--90
• Opis fizyczny: Bibliogr. 55 poz., rys.

Twórcy

autor

Piwowar M.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Lazarza 16, 31-530 Kraków, Poland

autor

Banach M.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Lazarza 16, 31-530 Kraków, Poland
• Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Reymonta 4, 30-059 Kraków, Poland

autor

Konieczny L.

• Chair of Medical Biochemistry, Jagiellonian University Medical College, Kopernika 7, 31-034 Kraków, Poland

autor

Chomilier J.

• IMPMC, Université Pierre et Marie Curie, CNRS, 4 Place Jussieu, Paris, France
• RPBS, 35 rue Hélène Brion, Paris, France

autor

Roterman I.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, Lazarza 16, 31-530 Kraków, Poland

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