Biomaterial Database

Interhelical contacts determining the architecture of alpha-helical globular proteins. 1994

I V Grigoriev, and A A Mironov, and A B Rakhmaninova

Department of Mathematical Modelling, Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia.

An approach based on a presentation of alpha-helical protein topology as a graph is presented. The approach allows to estimate a role of each interhelical contact in the whole protein topology and to classify the contacts. It is shown that a consideration of only about a half of the whole pool of interhelical contacts exposed in the protein is enough for a determination of protein architecture. Such contacts are called as major and their quantitative characteristics are obtained. Moreover, providing a clear and simple presentation of the protein topology, the approach can be applied for a description of structural domain/subdomain arrangement of alpha-helical proteins and illustration of their folding/denaturation paths.

UI	MeSH Term	Description	Entries
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D003626	Data Display	The visual representation of data via a manufactured system.	Information Display,Data Displays,Display, Data,Display, Information,Displays, Data,Displays, Information,Information Displays
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D017433	Protein Structure, Secondary	The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation.	Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D017510	Protein Folding	Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.	Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular