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- W638797 abstract "Typically, hydrophobic residues in proteins are found on the interior of the tertiary structure minimizing interactions with water. Many proteins function by exposing hydrophobic faces to the solvent. The molecule 1-anilinonaphthalene-8-sulfonic acid (1,8-ANS) will fluoresce exclusively in presence of hydrophobic interactions allowing investigation of exposed pockets in proteins. Two separate investigations with ANS and the proteins calmodulin and lysozyme are outlined. Calmodulin in the presence of calcium exposes two hydrophobic pockets which are accessible to ANS increasing the fluorescence signal compared to the absence of calcium. Lysozyme in the presence of varying the concentration of urea and ANS will produce a fluorescence maximum indicating a conformational structure exposing the hydrophobic core to solvent called the molten-globule state. These investigations are intended for an introductory laboratory in biochemistry." @default.
- W638797 created "2016-06-24" @default.
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- W638797 date "2009-04-01" @default.
- W638797 modified "2023-09-23" @default.
- W638797 title "Fluorescence investigation of hydrophobic pocket exposure in protein with 1‐anilinonaphthalene‐8‐sulfonic acid" @default.
- W638797 doi "https://doi.org/10.1096/fasebj.23.1_supplement.538.6" @default.
- W638797 hasPublicationYear "2009" @default.
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