Identification of helix capping and b-turn motifs from NMR chemical shifts.

ABSTRACT: We present an empirical method for identification of distinct structural motifs in proteins on the basis of experimentally determined backbone and (13)C(β) chemical shifts. Elements identified include the N-terminal and C-terminal helix capping motifs and five types of β-turns: I, II, I', II' and VIII. Using a database of proteins of known structure, the NMR chemical shifts, together with the PDB-extracted amino acid preference of the helix capping and β-turn motifs are used as input data for training an artificial neural network algorithm, which outputs the statistical probability of finding each motif at any given position in the protein. The trained neural networks, contained in the MICS (motif identification from chemical shifts) program, also provide a confidence level for each of the

SUBMITTER: Shen Y 

PROVIDER: S-EPMC3357447 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature