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Structural properties of semenogelin I.

Malm, Johan LU ; Jonsson, Magnus LU ; Frohm, Birgitta LU and Linse, Sara LU (2007) In The FEBS Journal 274(17). p.4503-4510
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
fertility, semen, semenogelin, zinc, structure
in
The FEBS Journal
volume
274
issue
17
pages
4503 - 4510
publisher
Federation of European Neuroscience Societies and Blackwell Publishing Ltd
external identifiers
  • wos:000248964100014
  • scopus:34548131166
ISSN
1742-464X
DOI
10.1111/j.1742-4658.2007.05979.x
language
English
LU publication?
yes
id
4394e537-2850-4c2c-862c-d2974c23aa0a (old id 607062)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17680810&dopt=Abstract
date added to LUP
2007-12-18 10:01:11
date last changed
2017-01-01 07:03:09
@article{4394e537-2850-4c2c-862c-d2974c23aa0a,
  abstract     = {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.},
  author       = {Malm, Johan and Jonsson, Magnus and Frohm, Birgitta and Linse, Sara},
  issn         = {1742-464X},
  keyword      = {fertility,semen,semenogelin,zinc,structure},
  language     = {eng},
  number       = {17},
  pages        = {4503--4510},
  publisher    = {Federation of European Neuroscience Societies and Blackwell Publishing Ltd},
  series       = {The FEBS Journal},
  title        = {Structural properties of semenogelin I.},
  url          = {http://dx.doi.org/10.1111/j.1742-4658.2007.05979.x},
  volume       = {274},
  year         = {2007},
}