Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 4 of 4
Full-Text Articles in Medicine and Health Sciences
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and for being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, to …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: I. Design And Analysis Of Monomeric Mutants, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, to …
Fluorescence Quantum Yield Of Thioflavin T In Rigid Isotropic Solution And Incorporated Into The Amyloid Fibrils, Anna I. Sulatskaya, Alexander A. Maskevich, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Fluorescence Quantum Yield Of Thioflavin T In Rigid Isotropic Solution And Incorporated Into The Amyloid Fibrils, Anna I. Sulatskaya, Alexander A. Maskevich, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
In this work, the fluorescence of thioflavin T (ThT) was studied in a wide range of viscosity and temperature. It was shown that ThT fluorescence quantum yield varies from 0.0001 in water at room temperature to 0.28 in rigid isotropic solution (T/η→0). The deviation of the fluorescence quantum yield from unity in rigid isotropic solution suggests that fluorescence quantum yield depends not only on the ultra-fast oscillation of ThT fragments relative to each other in an excited state as was suggested earlier, but also depends on the molecular configuration in the ground state. This means that the fluorescence …