Interconnection between the globule architecture and disposition of conformationally stanch oligopeptides in proteins of the same structural family

Autor:	Natalia G. Esipova, I. V. Filatov, A. V. Batyanovskii, Vladimir A. Namiot, I. D. Volotovsky
Rok vydání:	2012
Předmět:	chemistry.chemical_classification Oligopeptide Amino acid sequence homology Chemistry Globular protein Stereochemistry Structural similarity Biophysics Protein folding Macromolecule
Zdroj:	Biophysics. 57:831-834
ISSN:	1555-6654 0006-3509
Popis:	It has been shown that selective interactions between helical segments of macromolecules can be realized in globular proteins in the segments characterized by the same periodicities of charge distribution, i.e., conformationally stanch oligopeptides (CSOPs). It has been found that in the macromolecules of α-helical proteins, CSOPs are disposed at distances characteristic of direct interactions. For representatives of many structural families of α-type proteins, family-specific disposition of CSOPs is observed. The similar disposition of conformationally stanch segments is not related to amino acid sequence homology but reflects peculiarities of native 3D architectures of protein globules.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::39ca26924c948d17905df6dca0912561 https://doi.org/10.1134/s0006350912060024 Zobrazit plný text záznamu Full text from SpringerLink