Search Results - "Katina, N S"

Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram? by Balobanov, V. A., Katina, N. S., Finkelstein, A. V., Bychkova, V. E.

“…Several research teams have reported detection and characterization of various apomyoglobin intermediate states different in their accumulation mode, thus…”
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Kinetics of interactions between apomyoglobin and phospholipid membrane by Balobanov, V. A, Il'ina, N. B, Katina, N. S, Kashparov, I. A, Dolgikh, D. A, Bychkova, V. E

“…The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and circular dichroism in the far UV…”
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On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding by Baryshnikova (Samatova), E. N, Melnik, B. S, Balobanov, V. A, Katina, N. S, Finkelshtein, A. V, Semisotnov, G. V, Bychkova, V. E

“…The contributions of some amino acid residues in the A, B, G, and H helices to the formation of the folding nucleus and folding intermediate of apomyoglobin…”
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Identification of Regions in Apomyoglobin that Form Intermolecular Interactions in Amyloid Aggregates Using High-Performance Mass Spectrometry by Katina, N. S., Suvorina, M. Yu, Grigorashvili, E. I., Marchenkov, V. V., Ryabova, N. A., Nikulin, A. D., Surin, A. K.

“…The formation of amyloid aggregates in human organs and tissues causes the development of incurable diseases. However, experimental studies of the mechanism of…”
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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain by Katina, N. S., Grigorashvili, E. I., Suvorina, M. Yu, Ilyina, N. B., Ryabova, N. A., Selivanova, O. M., Surin, A. K.

“…As has been recently shown, the toxicity of protein aggregates is determined by their structure. Therefore, special attention has been focused on the search…”
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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain by Katina, N S, Grigorashvili, E I, Suvorina, M Yu, Ilyina, N B, Ryabova, N A, Selivanova, O M, Surin, A K

“…As has been recently shown, the toxicity of protein aggregates is determined by their structure. Therefore, special attention has been focused on the search…”
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Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature by Katina, N. S., Ilyina, N. B., Kashparov, I. A., Balobanov, V. A., Vasiliev, V. D., Bychkova, V. E.

“…Formation of amyloid-like protein aggregates in human organs and tissues underlies many serious diseases, therefore being in the focus of numerous biochemical,…”
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On the role of some conserved and nonconserved amino acid residues in transition state and in intermediate of apomyoglobin folding by Baryshnikova, E N, Mel'nik, B S, Katina, N S, Finkel'shteĭn, A V, Bychkova, V E

“…The effect of some amino acid residues in A, B, G, and H helices on the folding nucleus and folding intermediate state formation was estimated. For four…”
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Equilibrium unfolding of mutant apomyoglobins carrying substitutions of conserved nonfunctional residues with alanine by Baryshnikova, E. N., Balobanov, V. A., Katina, N. S., Melnik, B. S., Dolgikh, D. A., Semisotnov, G. V., Bychkova, V. E.

“…Protein aggregation or misfolding in the cell is connected with many genetic diseases and can result from substitutions in proteins. Substitutions can…”
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Kinetics of interaction between apomyoglobin and phospholipid membrane by Balobanov, V A, Il'ina, N B, Katina, N S, Kashparov, I A, Dolgikh, D A, Bychkova, V E

“…The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and CD in the far UV-region. It is…”
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Equilibrium unfolding of mutant apomyoglobins with substitutions of conserved nonfunctional residues by alanine by Baryshnikova, E N, Balobanov, V A, Katina, N S, Mel'nik, B S, Dolgikh, D A, Semisotnov, G V, Bychkov, V E

“…The problems of protein aggregation and protein misfolding in the cell are connected with the appearance of many genetic diseases. Both processes can be a…”
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