Avidin: Difference between revisions
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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
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3D structures of Avidin
Updated on 12-January-2016
Reference
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Michal Harel, Jaime Prilusky, Marcin Jozef Suskiewicz, Joel L. Sussman