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Portrait of Sara Snogerup Linse

Sara Linse

Professor

Portrait of Sara Snogerup Linse

Structural properties of semenogelin I.

Author

  • Johan Malm
  • Magnus Jonsson
  • Birgitta Frohm
  • Sara Linse

Summary, in English

The zinc-binding protein semenogelin I is the major structural component of the gelatinous coagulum that is formed in freshly ejaculated semen. Semenogelin I is a rapidly evolving protein with a primary structure that consists of six repetitive units, each comprising approximately 60 amino acid residues. We studied the secondary and tertiary structure of semenogelin I by circular dichroism (CD) spectroscopy and Trp fluorescence emission spectroscopy. Fitting to the far-UV CD data indicated that the molecule comprises 5-10%alpha-helix and 20-30%beta-sheet formations. The far-UV spectrum of semenogelin I is clearly temperature dependent in the studied range 5-90 degrees C, and the signal at 222 nm increased with increasing temperature. The presence of Zn2+ did not change the secondary structure revealed by the far-UV CD spectrum, whereas it did alter the near-UV CD spectrum, which implies that rearrangements occurred on the tertiary structure level. The conformational change induced in semenogelin I by the binding of Zn2+ may contribute to the ability of this protein to form a gel.

Department/s

  • Clinical Chemistry, Malmö
  • Biophysical Chemistry

Publishing year

2007

Language

English

Pages

4503-4510

Publication/Series

The FEBS Journal

Volume

274

Issue

17

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biochemistry and Molecular Biology

Keywords

  • fertility
  • semen
  • semenogelin
  • zinc
  • structure

Status

Published

Research group

  • Clinical Chemistry, Malmö

ISBN/ISSN/Other

  • ISSN: 1742-464X