Structural properties of semenogelin I.

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12 !!Citations (SciVal)
149 Nedladdningar (Pure)

Sammanfattning

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.
Originalspråkengelska
Sidor (från-till)4503-4510
TidskriftThe FEBS Journal
Volym274
Utgåva17
DOI
StatusPublished - 2007

Ämnesklassifikation (UKÄ)

  • Biokemi och molekylärbiologi

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