This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Avidin
From Proteopedia
(Difference between revisions)
| Line 23: | Line 23: | ||
The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | ||
| - | Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer. These <scene name=' | + | Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer. These <scene name='41/410356/Cv/14'>sugars</scene> appear along with the biotin but outside of the biotin binding pockets. |
See also:<br /> | See also:<br /> | ||
Revision as of 13:16, 12 January 2016
| |||||||||||
3D structures of Avidin
Updated on 12-January-2016
Reference
- Livnah O, Bayer EA, Wilchek M, Sussman JL. Three-dimensional structures of avidin and the avidin-biotin complex. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5076-80. PMID:8506353
- Livnah O, Bayer EA, Wilchek M, Sussman JL. The structure of the complex between avidin and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA). FEBS Lett. 1993 Aug 9;328(1-2):165-8. PMID:8344421
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Marcin Jozef Suskiewicz, Jaime Prilusky
