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A Distal Point Mutation in the Streptavidin-biotin Complex Preserves Structure but Diminishes Binding Affinity: Experimental Evidence for Electronic Polarization Effects?
We have identified a distal point mutation in streptavidin that causes a 1000-fold reduction in biotin binding affinity without disrupting the equilibrium complex structure. The F130L mutation creates a small cavity occupied by a water molecule, but all neighboring side chain positions are preserved...
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| Main Authors: | , , , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
2010
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2885148/ https://ncbi.nlm.nih.gov/pubmed/20462252 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi1005392 |
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