Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Maria A. Majorina"'
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
Publikováno v:
PLoS ONE, Vol 17, Iss 5 (2022)
Pseudomonas syringae is a widely spread plant pathogen known to have ice-nucleating proteins that serve as crystallization sites promoting ice growth at near-zero temperatures. Three temperatures that characterize water freezing and ice melting are (
Externí odkaz:
https://doaj.org/article/169425b8047c4249bdf516664f57fa48
Publikováno v:
FEBS lettersReferences. 594(20)
Apomyoglobin is a widely used model for studying the molecular mechanisms of globular protein folding. This work aimed to analyze the effects of rigidity and length of loops linking protein secondary structure elements on the stability of the molten
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6131b172720c629dfb9a59a589c2a31
https://pubmed.ncbi.nlm.nih.gov/32770670
https://pubmed.ncbi.nlm.nih.gov/32770670
Autor:
Maria A. Majorina, Bogdan S. Melnik
Apomyoglobin is a protein widely used as a model for studying globular protein folding. This work aimed to test the hypothesis on influence of rigidity and length of loops linking protein secondary structure elements on the stability of molten globul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e88d3523086afd4733012fc6c4130ac0
Autor:
Anatoly S. Glukhov, Ivan A. Kashparov, Daria S. Larina, Bogdan S. Melnik, Maria A. Majorina, Ekaterina Samatova, Tatiana N. Melnik
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e98645 (2014)
PLoS ONE, Vol 9, Iss 6, p e98645 (2014)
At present it is unclear which interactions in proteins reveal the presence of intermediate states, their stability and formation rate. In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydropho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bb3ab00e98fcab66f76a2d62945c8dd
https://doi.org/10.1371/journal.pone.0098645
https://doi.org/10.1371/journal.pone.0098645
Autor:
Tatiana N Melnik, Maria A Majorina, Daria S Larina, Ivan A Kashparov, Ekaterina N Samatova, Anatoly S Glukhov, Bogdan S Melnik
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98645 (2014)
At present it is unclear which interactions in proteins reveal the presence of intermediate states, their stability and formation rate. In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydropho
Externí odkaz:
https://doaj.org/article/790183bf70a74d40ac87c4ce8fddddd4