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NMR Structure and Dynamics of the Engineered Fluorescein-Binding Lipocalin FluA Reveals Rigidification of β-Barrel and Variable Loops upon Enthalpy-Driven Ligand Binding
The NMR structure of the 21 kDa lipocalin FluA, which was previously obtained by combinatorial design, elucidates a reshaped binding site specific for the dye fluorescein resulting from 21 side chain replacements with respect to the parental lipocalin, the naturally occurring bilin-binding protein (...
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| Main Authors: | , , , |
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| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
2009
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2860743/ https://ncbi.nlm.nih.gov/pubmed/19603796 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi900535j |
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