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Dissimilar sequence: similar structure of proteins

Identyfikatory
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Sequence-to-structure relation is one of the major objects of the analysis of protein folding problem. The pair of two small proteins (domains) of similar structure (β-hairpin/α-helix/β-hairpin) generated by the chains of similar length (about 60 amino acids) with very low sequence similarity (15%) is the object of the comparable analysis of 3D structure. The criterion for similarity estimation is the status of polypeptide chain with respect to the hydrophobic core structure. The fuzzy oil drop model is applied to reveal the differentiated status of fragments of the well-defined secondary structure. This analysis allows the interpretation of the structure in other than the geometric form as it is made based on secondary structure classification. The two compared highly similar proteins appear to be different with respect to the hydrophobic core structure.
Rocznik
Strony
117--121
Opis fizyczny
Bibliogr. 14 poz., rys., wykr.
Twórcy
autor
  • Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-530 Krakow, Łazarza 16, Poland
autor
  • Medical Biochemistry, Jagiellonian University Medical College, 31-034 Krakow, Kopernika 7, Poland
autor
  • Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-530 Krakow, Łazarza 16, Poland
Bibliografia
  • 1. Dill KA, MacCallum JL. The protein-folding problem, 50 years on. Science 2012;338:1042–6.
  • 2. Moult J, Fidelis K, Kryshtafovych A, Schwede T, Tramontano A. Critical assessment of methods of protein structure prediction (CASP) – round x. Proteins 2014;82:1–6.
  • 3. Allison JR, Bergeler M, Hansen N, van Gunsteren WF. Current computer modeling cannot explain why two highly similar sequences fold into different structures. Biochemistry 2011;50:10965–73.
  • 4. Khoury GA, Liwo A, Khatib F, Zhou H, Chopra G, Bacardit J, et al. WeFold: a coopetition for protein structure prediction. Proteins 2014;82:1850–68.
  • 5. Konieczny L, Bryliński M, Roterman I. Gauss-function-based model of hydrophobicity density in proteins. In Silico Biol 2006;6:15–22.
  • 6. Gallagher T, Alexander P, Bryan P, Gilliland GL. Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 1994;33:4721–9.
  • 7. O’Neill JW, Kim DE, Baker D, Zhang KY. Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution. Acta Crystallogr D Biol Crystallogr 2001;57:480–7.
  • 8. Levitt MA. A simplified representation of protein conformations for rapid simulation of protein folding. J Mol Biol 1976;104:59–107.
  • 9. Kullback S, Leibler RA. On information and sufficiency. Ann Math Stat 1951;22:79–86.
  • 10. Kalinowska B, Banach M, Konieczny L, Roterman I. Application of divergence entropy to characterize the structure of the hydrophobic core in DNA interacting proteins. Entropy 2015;17:1477–507.
  • 11. Kalinowska B, Banach M, Konieczny L, Marchewka D, Roterman I. Intrinsically disordered proteins – relation to general model expressing the active role of the water environment. Adv Protein Chem Struct Biol 2014;94:315–46.
  • 12. Banach M, Konieczny L, Roterman I. The fuzzy oil drop model, based on hydrophobicity density distribution, generalizes the influence of water environment on protein structure and function. J Theor Biol 2014;359:6–17.
  • 13. Banach M, Prudhomme N, Carpentier M, Duprat E, Papandreou N, Kalinowska B, et al. Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases. PLoS One 2015;10:e0125098.
  • 14. Banach M, Kalinowska B, Konieczny L, Roterman I. Role of disulfide bonds in stabilizing the conformation of selected enzymes – an approach based on divergence entropy applied to the structure of hydrophobic core in proteins. Entropy 2016;18:67.
Uwagi
Opracowanie ze środków MNiSW w ramach umowy 812/P-DUN/2016 na działalność upowszechniającą naukę.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-805d1962-8f23-4b1e-b11f-d23fbd75ea06
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