Author

B. S. Melnik

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Bioengineering· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Research Focus:protein design· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

K. A. Glukhova· 2 shared M. A. Majorina· 2 shared A. V. Finkelstein· 1 shared D. E. Vorobeva· 1 shared E. A. Sokolova· 1 shared I. V. Balalaeva· 1 shared N. Y. Marchenko· 1 shared V. G. Klyashtorny· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

8 top collaborators · 10 mutual co-author links

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2 shared papersBiophysics

K. A. Glukhova

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Investigation of ice nucleation properties of Pseudomonas syringae bacterium and insoluble low molecular weight substances

D. E. Vorobeva, M. A. Majorina, N. Y. Marchenko, B. S. Melnik

This study investigates the ice nucleation properties of Pseudomonas syringae and insoluble low molecular weight substances, finding that AgCl, ZnO, and SnO2 act as ice nucleators.

bioRxiv · Dec 9, 2023 · PreprintBiophysics

A novel view on the mechanism of biological activity of antifreeze proteins

B. S. Melnik, K. A. Glukhova, E. A. Sokolova, I. V. Balalaeva, A. V. Finkelstein

This paper challenges the common belief about antifreeze proteins by showing they raise ice melting points and prevent ice formation by binding to cell surfaces rather than ice crystals.

bioRxiv · Sep 22, 2021 · PreprintBiophysics

Loops linking secondary structure elements affect the stability of molten globule intermediate state of apomyoglobin

M. A. Majorina, B. S. Melnik

This study investigates how loop rigidity and length in apomyoglobin affect the stability of its molten globule intermediate state through mutagenesis and thermodynamic analysis.

bioRxiv · Nov 27, 2019Biophysics

GFP fusion protein with embedded foreign peptide

K. A. Glukhova, V. G. Klyashtorny, B. S. Melnik

This study explores using GFP's structure to encapsulate foreign peptides, showing that a modified GFP with an antimicrobial peptide is compact and non-toxic but structurally unstable.

bioRxiv · Nov 26, 2019 · PreprintBioengineering