Flexible structures and ligand interactions of tandem repeats consisting of proline, glycine, asparagine, serine, and/or threonine rich oligopeptides in proteins

• Published in: Current protein & peptide science Vol. 9; no. 6; p. 591
• Main Authors: Matsushima, Norio, Yoshida, Hitoshi, Kumaki, Yasuhiro, Kamiya, Masakatsu, Tanaka, Takanori, Izumi, Yoshinobu, Kretsinger, Robert H
• Format: Journal Article
• Language: English
• Published: United Arab Emirates 01.12.2008
• Subjects: Animals; Asparagine - chemistry; Asparagine - metabolism; Glycine - chemistry; Glycine - metabolism; Humans; Ligands; Oligopeptides - chemistry; Oligopeptides - metabolism; Proline - chemistry; Proline - metabolism; Protein Conformation; Proteins - chemistry; Proteins - metabolism; Serine - chemistry; Serine - metabolism; Tandem Repeat Sequences; Threonine - chemistry; Threonine - metabolism

Tandem repeats occur in 14% of all proteins. The repeat unit lengths range from a single amino acid to more than 100 residues and the repeat number is sometimes over 100. Understanding the structures, functions, and evolution of these repeats is a significant goal in both proteomics and genomics. Th...