The design of antiparallel coiled coils.
Recent structural studies have highlighted the importance of antiparallel coiled coils in nature. In addition, well-behaved, model antiparallel coiled coils have been designed and used for the reassembly of protein fragments and for the study of the energetic contributions of various interactions to helix orientation specificity. Finally, high-resolution structural data are available for designed helical bundles, allowing an evaluation of the success of state-of-the-art protein design efforts.
Oakley
M G
MG
Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA. oakley@indiana.edu
Hollenbeck
J J
JJ
D000465:Algorithms; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D016208:Databases, Factual; D005544:Forecasting; D018963:Hepatitis Antigens / Q000737:chemistry; D035923:Hepatitis delta Antigens; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011493:Protein Kinase C; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D011505:Protein-Tyrosine Kinases / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry; D012714:Serine-tRNA Ligase / Q000737:chemistry; D013049:Spectrin / Q000737:chemistry
D001426:Bacterial Proteins; D018963:Hepatitis Antigens; D035923:Hepatitis delta Antigens; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid; D013049:Spectrin; C061570:protein kinase N; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C; D012714:Serine-tRNA Ligase