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Spatial structure of fibrinopeptide B in water solution with DPC micelles by NMR spectroscopy
Blokhin D., Fayzullina A., Filippov A., Karataeva F., Klochkov V.
. In this article, GluFib peptide is investigated together with dodecylphosphocholine (DPC) micelles which were used
High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles
Usachev K., Efimov S., Kolosova O., Filippov A., Klochkov V.
in dodecylphosphocholine (DPC) micelles, and a channel is formed by the association of several dimers but the molecular
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: A high-resolution NMR study
Usachev K., Efimov S., Kolosova O., Klochkova E., Aganov A., Klochkov V.
of perdeuterated DPC micelles and demonstrate that PG-3 forms an antiparallel NCCN dimer with a possible
High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles
Usachev K., Efimov S., Kolosova O., Filippov A., Klochkov V.
in dodecylphosphocholine (DPC) micelles, and a channel is formed by the association of several dimers but the molecular
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: A high-resolution NMR study
Usachev K., Efimov S., Kolosova O., Klochkova E., Aganov A., Klochkov V.
of perdeuterated DPC micelles and demonstrate that PG-3 forms an antiparallel NCCN dimer with a possible
The Affect of Gadolinium Ion on Micelles and Reverse Micelles by NMR Spectroscopy
Tarasov A.S., Rakhmatullin I.Z., Shurshalova G.S., Klochkov A.V., Il’yasov K.A., Klochkov V.V.
of the interaction between paramagnetic gadolinium ions and membrane models using micelles based
Spatial structure of fibrinopeptide B in water solution with DPC micelles by NMR spectroscopy
Blokhin D., Fayzullina A., Filippov A., Karataeva F., Klochkov V.
. In this article, GluFib peptide is investigated together with dodecylphosphocholine (DPC) micelles which were used
The effect of the detergent micelles type on the tetrapeptide NAc-SFVG-OMe conformational structure: NMR studies in solution
Usachev K., Klochkova E., Yulmetov A., Klochkov V.
such as DPC are used to mimic eukaryote membranes while the negatively charged SDS micelles would resemble
Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles
Sanchugova D.A., Bikmullin A.G., Klochkov V.V., Aganov A.V., Blokhin D.S.
in an aqueous solution containing dodecylphosphocholine (DPC) micelles by NMR spectroscopy. It was found
The effect of the detergent micelles type on the tetrapeptide NAc-SFVG-OMe conformational structure: NMR studies in solution
Usachev K., Klochkova E., Yulmetov A., Klochkov V.
such as DPC are used to mimic eukaryote membranes while the negatively charged SDS micelles would resemble

Страница 1 из 45

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