On the Number of Independent Sets in Simple Hypergraphs von Balobanov, A. E., Shabanov, D. A.

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The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception von Bychkova, Valentina E., Dolgikh, Dmitry A., Balobanov, Vitalii A., Finkelstein, Alexei V.

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Function of the Conserved Non-Functional Residues in Apomyoglobin – to Determine and to Preserve Correct Topology of the Protein von Bychkova, Valentina E., Dolgikh, Dmitry A., Balobanov, Vitalii A.

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The Molten Globule Concept: 45 Years Later von Bychkova, V. E., Semisotnov, G. V., Balobanov, V. A., Finkelstein, A. V.

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Formation of the Native Topology of a Protein is due to the "Conserved but Non-Functional" Residues: A Case of Apomyoglobin Folding von Bychkova, Valentina E, Dolgikh, Dmitry A, Balobanov, Vitalii A, Finkelstein, Alexei V

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On the strong chromatic number of a random 3-uniform hypergraph von Balobanov, Arseniy E., Shabanov, Dmitry A.

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How membrane surface affects protein structure von Bychkova, V. E., Basova, L. V., Balobanov, V. A.

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sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability von Katina, Natalya S., Balobanov, Vitalii A., Ilyina, Nelly B., Vasiliev, Victor D., Marchenkov, Victor V., Glukhov, Anatoly S., Nikulin, Alexey D., Bychkova, Valentina E.

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

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Folding Intermediate and Folding Nucleus for I→N and U→I→N Transitions in Apomyoglobin: Contributions by Conserved and Nonconserved Residues von Samatova, Ekaterina N., Melnik, Bogdan S., Balobanov, Vitaly A., Katina, Natalya S., Dolgikh, Dmitry A., Semisotnov, Gennady V., Finkelstein, Alexei V., Bychkova, Valentina E.

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Estimation of residual stresses in locomotive wheel treads using the acoustoelasticity method von Murav’ev, V. V., Volkova, L. V., Balobanov, E. N.

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Membrane-induced changes in the holomyoglobin tertiary structure: interplay with function von Basova, Liana V., Tiktopulo, Elisaveta I., Kutyshenko, Victor P., Klenin, Stanislav I., Balobanov, Vitalii A., Bychkova, Valentina E.

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Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature von Katina, N. S., Ilyina, N. B., Kashparov, I. A., Balobanov, V. A., Vasiliev, V. D., Bychkova, V. E.

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How strong are side chain interactions in the folding intermediate? von Samatova, Ekaterina N., Katina, Natalia S., Balobanov, Vitaly A., Melnik, Bogdan S., Dolgikh, Dmitry A., Bychkova, Valentina E., Finkelstein, Alexei V.

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Fusion Proteins are Able to Form Amyloid Structure von Balobanov, Vitaly A., Egorova, Anna G., Chertkova, Rita V., Ilyina, Nelly B., Vasilyev, Victor D., Bychkova, Valentina E.

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The Effect of Protein Stability on Interactions of Apomyoglobin Forms with Phospholipid Membranes von Balobanov, Vitaly A., Ilyina, Nelly B., Katina, Natalia S., Kashparov, Ivan A., Bychkova, Valentina E.

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Kinetics of interactions between apomyoglobin and phospholipid membrane von Balobanov, V. A, Il'ina, N. B, Katina, N. S, Kashparov, I. A, Dolgikh, D. A, Bychkova, V. E

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pH-induced equilibrium unfolding of apomyoglobin: Substitutions at conserved Trp14 and Met131 and non-conserved Val17 positions von Dyuysekina, A. E., Dolgikh, D. A., Samatova, E. N., Tiktopulo, E. I., Balobanov, V. A., Bychkova, V. E.

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Possible Mechanism Of Amyloid Formation By Apomyoglobin Mutants von Katina, Natalia S., Dudina, Maria A., Balobanov, Vitaly A., Samatova, Ekaterina N., Bychkova, Valentina E.

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Point Substitution in Albebetin Sequence Accelerates the Amyloid Structure Formation von Balobanov, Vitaly A., Anisimov, Yakov S., Chertkova, Rita V., Ilyina, Nelly B., Vasilyev, Victor D., Bychkova, Valentina E.

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