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What macromolecular crowding can do to a protein
Kuznetsova I.M.
crowding might affect protein structure, folding, shape, conformational stability, binding of small
HDL phospholipid: A natural inhibitor of Alzheimer's amyloid β-fibrillogenesis? [2]
Koudinov A.R., Koudinova N.V., Berezov T.T., Ivanov Y.D.
protein secondary structure
The native monomer of bacillus pumilus ribonuclease does not exist extracellularly
Ilinskaya O.
of binase. The immutability of binase secondary structure upon transition from low to high protein
New insight into secreted ribonuclease structure: Binase is a natural dimer
Dudkina E.
New insight into secreted ribonuclease structure: Binase is a natural dimer
Prime-boost vaccination with a combination of proteosome-degradable and wild-type forms of two influenza proteins leads to augmented CTL response
Ilyinskii P.O.
-cell cross-presentation by APCs, a mechanism that requires high levels of the antigenic protein. Therefore
NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome
Mariasina S., Petrova O., Osterman I., Sergeeva O., Efimov S., Klochkov V., Sergiev P., Dontsova O., Huang T., Chang C., Polshakov V.
of the assigned chemical shifts allowed us to characterize the protein’s secondary structure and backbone dynamics
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase
Polshakov V., Petrova O., Parfenova Y., Efimov S., Klochkov V., Zvereva M., Dontsova O.
shifts allowed us to identify secondary structures and protein regions potentially involved
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase
Polshakov V., Petrova O., Parfenova Y., Efimov S., Klochkov V., Zvereva M., Dontsova O.
of the assigned chemical shifts allowed us to identify secondary structures and protein regions potentially
Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha
Mariasina S., Efimov S., Petrova O., Rodina E., Malyavko A., Zvereva M., Klochkov V., Dontsova O., Polshakov V.
to identify the protein’s secondary structure and backbone dynamic properties. Structure-based sequence
Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage
Bogachev M., Kayumov A., Markelov O., Bunde A.
Structural, localization and functional properties of unknown proteins are often being predicted

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