Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Galina S. Nagibina"'
Autor:
Tatiana N. Melnik, Maria A. Majorina, Daria E. Vorobeva, Galina S. Nagibina, Victoria R. Veselova, Ksenia A. Glukhova, Marina A. Pak, Dmitry N. Ivankov, Vladimir N. Uversky, Bogdan S. Melnik
Publikováno v:
Cell Communication and Signaling, Vol 22, Iss 1, Pp 1-14 (2024)
Abstract Enhancing protein stability holds paramount significance in biotechnology, therapeutics, and the food industry. Circular permutations offer a distinctive avenue for manipulating protein stability while keeping intra-protein interactions inta
Externí odkaz:
https://doaj.org/article/9410afd45a174dc8be20500740b5422c
Autor:
Galina S. Nagibina, Ksenia A. Glukhova, Vladimir N. Uversky, Tatiana N. Melnik, Bogdan S. Melnik
Publikováno v:
Biomolecules, Vol 10, Iss 1, p 64 (2019)
Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. This work summarizes our research on the effect of amino acid substitutions on the protein stab
Externí odkaz:
https://doaj.org/article/41e7d4a2ba5e4bacb4b137f404936f51
Autor:
Tatiana N. Melnik, Bogdan S. Melnik, Ksenia A Glukhova, Galina S. Nagibina, Vladimir N. Uversky
Publikováno v:
Biomolecules
Volume 10
Issue 1
Biomolecules, Vol 10, Iss 1, p 64 (2019)
Volume 10
Issue 1
Biomolecules, Vol 10, Iss 1, p 64 (2019)
Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. This work summarizes our research on the effect of amino acid substitutions on the protein stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d166462e67f078f5ee38acb56b0edcc
https://pubmed.ncbi.nlm.nih.gov/32828465
https://pubmed.ncbi.nlm.nih.gov/32828465
Autor:
Galina S. Nagibina, Ksenia A Glukhova, Bogdan S. Melnik, Tatiana N. Melnik, Victor V. Marchenkov
Publikováno v:
Biochemistry. Biokhimiia. 85(1)
In our previous papers, we proposed the idea that programs predicting intrinsically disordered regions in amino acid sequences can be used for finding weakened sites in proteins. The regions predicted by such programs are suitable targets for the int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5992141cccf6a2ff6bb0ec4d159849e9
https://pubmed.ncbi.nlm.nih.gov/32079520
https://pubmed.ncbi.nlm.nih.gov/32079520
Autor:
Bogdan S. Melnik, Ksenia A Glukhova, Vladimir N. Uversky, Tatiana N. Melnik, Galina S. Nagibina
Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. In this work, we have successfully used algorithms for the evaluation of intrinsic disorder pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a4e4583e2ff7f9cf6a48c75798dd353
https://doi.org/10.1016/bs.pmbts.2020.05.005
https://doi.org/10.1016/bs.pmbts.2020.05.005
Publikováno v:
Molecular Biology. 52:75-83
Studying the effect of cysteine bridges on different energy levels of multistage folding proteins will enable a better understanding of the process of folding and functioning of globular proteins. In particular, it will create prospects for directed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9250bd99bbbd4309a909c6cc781864f6
https://doi.org/10.1134/s0026893318010120
https://doi.org/10.1134/s0026893318010120
Autor:
Tatiana N. Melnik, Bogdan S. Melnik, Anatoly S. Glukhov, Galina S. Nagibina, Vladimir N. Uversky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864:1809-1817
Various effects of amino acid substitutions on properties of globular proteins have been described in a large number of research papers. Nevertheless, no definite "rule" has been formulated as of yet that could be used by experimentalists to introduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09b5f713695210f9364767afc4ca7b3d
https://doi.org/10.1016/j.bbapap.2016.09.006
https://doi.org/10.1016/j.bbapap.2016.09.006
Publikováno v:
Biophysics. 61:860-870
An experimental approach named μ-analysis has been developed in order to elucidate the sequence of the loss of ordered structure by elements of a protein during the denaturation of the molecule. This approach is applicable for the analysis of protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e50e61b5b04ec80dce213e2c0eb04292
https://doi.org/10.1134/s0006350916060178
https://doi.org/10.1134/s0006350916060178
Publikováno v:
Protein & Peptide Letters. 23:176-184
In this study, we have used an approach that allows us to determine in what region of the polypeptide chain of protein it is required to insert a disulphide bond in order to stabilize it. In our previous paper [Melnik et al., JBSD. 2012] it was propo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bccc25fbb5b96c6bdc604e1e7456eda7
https://doi.org/10.2174/092986652302160105130540
https://doi.org/10.2174/092986652302160105130540
Publikováno v:
Vestnik of Saint Petersburg University. Physics. Chemistry. 3:288-295
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0493f475ceec333b33c67ed40bb50a0
https://doi.org/10.21638/11701/spbu04.2016.305
https://doi.org/10.21638/11701/spbu04.2016.305