Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.
It is a unique trait of the NMR method for protein structure determination that a description of the polypeptide secondary structure can be obtained at an early stage and quite independently of the complete structure calculation. In this paper the procedures used for secondary structure determination are reviewed and placed in perspective relative to the other steps in a complete three-dimensional structure determination. As an illustration the identification of the regular secondary structure elements in human cyclophilin is described.
Wüthrich
K
K
Institut für Molekularbiologie und Biophysik, ETH Hönggerberg, Zürich, Switzerland.
Spitzfaden
C
C
Memmert
K
K
Widmer
H
H
Wider
G
G
D000591:Amino Acid Isomerases / Q000737:chemistry*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D002352:Carrier Proteins; D011994:Recombinant Proteins; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase