File:Dimerization site GSS.jpg: Difference between revisions

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Shown in purple is the site of dimerization formed by the two homogenous protein subunits.
 
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Shown in purple is the site of dimerization formed by the two homogenous protein subunits.
Shown in purple is the site of dimerization formed by the two homogenous protein subunits.
Image borrowed from the NCBI databank for non-profit and educational purposes only. I claim no credit for the image shown. All credit goes to Slavens, et al (2011) at the following article:
Slavens KD, Brown TR, Barakat KA, Cundari TR, Anderson ME. 2011. Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity. Biochem & Biophys Resear Comm, 410(3): 597-601. doi: 10.1016/j.bbrc.2011.06.034

Latest revision as of 14:22, 5 December 2013

Shown in purple is the site of dimerization formed by the two homogenous protein subunits.

Image borrowed from the NCBI databank for non-profit and educational purposes only. I claim no credit for the image shown. All credit goes to Slavens, et al (2011) at the following article:

Slavens KD, Brown TR, Barakat KA, Cundari TR, Anderson ME. 2011. Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity. Biochem & Biophys Resear Comm, 410(3): 597-601. doi: 10.1016/j.bbrc.2011.06.034

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current01:09, 5 December 2013Thumbnail for version as of 01:09, 5 December 20131,050 × 689 (390 KB)Elliott Wyatt (talk | contribs)Shown in purple is the site of dimerization formed by the two homogenous protein subunits.

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Elliott Wyatt