The structure and function of proline-rich regions in proteins.
Williamson
M P
MP
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000502:physiology; D066246:ErbB Receptors / Q000378:metabolism; D005419:Flavonoids; D006909:Hydroxyproline / Q000737:chemistry; D008565:Membrane Proteins / Q000502:physiology; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D010636:Phenols / Q000378:metabolism; D011108:Polymers / Q000378:metabolism; D059808:Polyphenols; D011392:Proline / Q000737:chemistry*; D055232:Proline-Rich Protein Domains; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012319:RNA Polymerase II / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D012471:Salivary Proteins and Peptides / Q000378:metabolism; D013816:Thermodynamics
D001426:Bacterial Proteins; D005419:Flavonoids; D008565:Membrane Proteins; D010455:Peptides; D010636:Phenols; D011108:Polymers; D059808:Polyphenols; D012471:Salivary Proteins and Peptides; C057616:tonB protein, Bacteria; D011392:Proline; D066246:ErbB Receptors; D012319:RNA Polymerase II; D006909:Hydroxyproline