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:
https://lup.lub.lu.se/record/607062
- author
- Malm, Johan
LU
; Jonsson, Magnus
LU
; Frohm, Birgitta
LU
and Linse, Sara
LU
- organization
- publishing date
- 2007
- 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
- Wiley-Blackwell
- 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
- 2016-04-01 16:21:44
- date last changed
- 2022-01-28 19:12:13
@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}},
keywords = {{fertility; semen; semenogelin; zinc; structure}},
language = {{eng}},
number = {{17}},
pages = {{4503--4510}},
publisher = {{Wiley-Blackwell}},
series = {{The FEBS Journal}},
title = {{Structural properties of semenogelin I.}},
url = {{https://lup.lub.lu.se/search/files/4649498/626109.pdf}},
doi = {{10.1111/j.1742-4658.2007.05979.x}},
volume = {{274}},
year = {{2007}},
}