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Your search keyword '"Fomenkova NP"' showing total 4 results
Start Over Author "Fomenkova NP" Journal molekuliarnaia biologiia
4 results on '"Fomenkova NP"'

1. [Ribosomal structure: RNA-protein and protein-protein interactions].

Author

Nikonov SV, Fomenkova NP, Nikulin AD, Fedorov RV, and Nevskaia NA

Subjects
Base Sequence, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, RNA, Ribosomal chemistry, Ribosomal Proteins chemistry, Ribosomal Proteins metabolism, RNA, Ribosomal metabolism, RNA-Binding Proteins metabolism, Ribosomes
Published
1998

2. [Structural aspects of protein thermostability].

Author

Fomenkova NP, Nevskaia NA, Nikulin AD, and Nikonov SV

Subjects
Amino Acid Sequence, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Thermodynamics, Bacterial Proteins chemistry, Ribosomal Proteins chemistry
Published
1998

4. [Evolutionary conservatism of the molecular structure of gamma-crystallins of vertebrates].

Author

Chirgadze IuN, Nevskaia NA, Sergeev IuV, and Fomenkova NP

Subjects
Amino Acid Sequence, Animals, Humans, Models, Molecular, Protein Conformation, Biological Evolution, Crystallins, Vertebrates
Abstract

Homology of 18 amino acid sequences of lens gamma-crystallins of several vertebrates: frog, mouse, rat, calf and human being--has been considered. Pair sequence homology varies in the range from 57 to 100%, the mean value is equal to 74%. The spatial structures have been determined only for two calf gamma-crystallins. The protein molecule consists of four-fold repeated "motifs" (patterns) which are joint in two domains. After comparison of 18 gamma-crystallin sequences it was found that "motifs" domains and whole protein molecules have about 10, 30 and 58% conservative residues, respectively, that seem to be related to the evolution of these structural units. Structure analysis shows that almost all the conservative residues have an important structural meaning and play a basic role in the domain and molecular structure organization. This result allows us to make a conclusion about the homology of spatial structures of all considered gamma-crystallins of vertebrates.

Published
1987

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