Biomaterial Database

[Structure of alpha-spiral hairpins with short connections in globular proteins]. 2001

E V Brazhnikov, and A V Efimov

The analysis of conformations of more than 100 alpha-alpha-hairpins with closely packed helical segments and connections up to four amino acid residues in length was carried out. Five types of the connections were revealed and their phi and psi values on the Ramachandran map were found. Each type of alpha-alpha-hairpins was shown to have a unique sequence pattern for hydrophobic and hydrophilic residues.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
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
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene