Melting of the left-handed helical conformation of charged poly-L-lysine.
Authors: Makarov AA, Adzhubei IA, Protasevich II, Lobachov VM, Fasman GD.
Biopolymers
View full abstract on Pubmed
Biopolymers
View full abstract on Pubmed
Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.
Authors: Makarov AA, Adzhubei IA, Protasevich II, Lobachov VM, Esipova NG.
J Protein Chem
View full abstract on Pubmed
J Protein Chem
View full abstract on Pubmed
[Study of the conformational properties of C-terminal fragments of histones H1, H5, and beta-endorphin by circular dichroism].
Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin.
Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a contranslational protein-folding model.
[Microcalorimetric study of polypeptides in the conformation of the left helix of the poly-L-proline II type].
Authors: Makarov AA, Protasevich II, Adzhubei IA, Esipova NG.
Biofizika
View full abstract on Pubmed
Biofizika
View full abstract on Pubmed
[Role of the code redundancy in determining cotranslational protein folding].
[Frequency of using codons in mRNA and coding of the domain structure of proteins].
[Role of the rare codon clusters in defining the boundaries of polypeptide chain regions with identical secondary structures in the process of co-translational folding of proteins].
2002.
Authors: MDB: A new generation relational structure database implementing mmCIF approaches