The nitrogenase MoFe protein. A secondary structure prediction.
Surface residues, interior residues, and parsing residues, together with a secondary structure derived from these, are predicted for the MoFe nitrogenase protein in advance of a crystal structure of the protein, scheduled shortly to appear in Nature. By publishing this prediction, we test our method for predicting the conformation of proteins from patterns in the divergent evolution of homologous protein sequences in a way that places the method 'at risk'.
Gerloff
D L
DL
Laboratory for Organic Chemistry, ETH Zürich, Switzerland.
Jenny
T F
TF
Knecht
L J
LJ
Gonnet
G H
GH
Benner
S A
SA
D000595:Amino Acid Sequence; D016948:Azotobacter vinelandii / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000648:ultrastructure; D003461:Crystallography; D007501:Iron; D008667:Metalloproteins / Q000737:chemistry / Q000648:ultrastructure; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D008982:Molybdenum; D009591:Nitrogenase / Q000737:chemistry* / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D001426:Bacterial Proteins; D008667:Metalloproteins; D008982:Molybdenum; D007501:Iron; D009591:Nitrogenase