Title : Three-dimensional structure and position of porcine motilin in sodium dodecyl sulfate micelles determined by 1H NMR.

Pub. Date : 1997 Jul 1

PMID : 9201964






5 Functional Relationships(s)
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1 Three-dimensional structure and position of porcine motilin in sodium dodecyl sulfate micelles determined by 1H NMR. Sodium Dodecyl Sulfate motilin Homo sapiens
2 The solution structure of the porcine gastrointestinal peptide hormone motilin was determined in the presence of sodium dodecyl sulfate (SDS) micelles at 28 degrees C using 1H nuclear magnetic resonance, full relaxation matrix analysis, and structure calculations based on restrained molecular dynamics. Sodium Dodecyl Sulfate motilin Homo sapiens
3 The solution structure of the porcine gastrointestinal peptide hormone motilin was determined in the presence of sodium dodecyl sulfate (SDS) micelles at 28 degrees C using 1H nuclear magnetic resonance, full relaxation matrix analysis, and structure calculations based on restrained molecular dynamics. Sodium Dodecyl Sulfate motilin Homo sapiens
4 The structure of motilin in SDS micelles is described by a reverse gamma-turn and a beta-turn of type II in the N terminal end, an alpha-helical region in the middle of the molecule, and an extended structure at the C terminus. Sodium Dodecyl Sulfate motilin Homo sapiens
5 The long correlation time in combination with a high order parameter (S = 0.92) indicates that motilin has a rigid structure in the complex with the SDS micelle. Sodium Dodecyl Sulfate motilin Homo sapiens