Solution structure of seminal plasmin in the presence of micelles.
The 47-amino-acid peptide seminal plasmin maintains a random-coil characteristic feature when in aqueous solution, as can be shown by CD and NMR measurements. However, upon binding to a hydrophobic/hydrophilic interface, an increase in the content of secondary structure is observed. This change in conformation can also be induced with the addition of a detergent. The secondary structure segments thus formed were assigned by two-dimensional NMR. The results indicate that hydrophobic interactions are a driving force in the folding of seminal plasmin. The interaction of seminal plasmin with detergent micelles could serve as a model for the binding of this interesting protein with the acrosome membrane of sperm cells.
Maurer
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Institut für Biophysikalische Chemie, Biozentrum der Johann-Wolfgang-Goethe-Universität, Frankfurt am Main, Germany.
Rüterjans
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D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003902:Detergents; D005341:Fibrinolysin / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008823:Micelles; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010767:Phosphorylcholine / Q000031:analogs & derivatives; D010777:Photochemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012661:Semen / Q000201:enzymology*; D012996:Solutions; D014867:Water
D003902:Detergents; D008823:Micelles; D012996:Solutions; D014867:Water; D010767:Phosphorylcholine; C028810:dodecylphosphocholine; D005341:Fibrinolysin