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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
This new method for rapidly and quantitatively determining the identity, extent, and location of secondary structural elements in proteins based on the simple inspection of the alpha-CH 1H resonance assignments is found to be almost as accurate as the more traditional NOE-based methods of determining secondary structure.
A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
Molecular models for the voltage-gated ion channel, with n-fold symmetry and based on the molecular conformations observed in the crystal, are characterized by strong surface complementarity, aHydrophilic interior and a hydrophobic exterior.
An efficient newton‐like method for molecular mechanics energy minimization of large molecules
Techniques from numerical analysis and crystallographic refinement have been combined to produce a variant of the Truncated Newton nonlinear optimization procedure. The new algorithm shows particular
Identification of structural motifs from protein coordinate data: Secondary structure and first‐level supersecondary structure *
A computer program is described that produces a description of the secondary structure and supersecondary structure of a polypeptide chain using the list of alpha carbon coordinates as input and assigns 90–95% of the residues in most proteins to at least one type of secondary element.
1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type.
Ten samples of Escherichia coli thioredoxin were individually isotopically enriched by residue type via growth of an appropriate auxotrophic strain on media supplemented with one 2H, 15N-enriched amino acid through 1H observe-heteronuclear decoupling experiments making use of the 95-Hz 1H-15N amide J1 coupling.