Solvation dynamics in a protein–surfactant complex

✍ Scribed by Partha Dutta; Pratik Sen; Arnab Halder; Saptarshi Mukherjee; Sobhan Sen; Kankan Bhattacharyya

• Publisher: Elsevier Science
• Year: 2003
• Tongue: English
• Weight: 216 KB
• Volume: 377
• Category: Article
• ISSN: 0009-2614
• DOI: 10.1016/s0009-2614(03)01143-6

✦ Synopsis

Solvation dynamics in the denatured state of a protein, lysozyme (denatured by sodium dodecyl sulfate, SDS) is markedly slower than that in the native state. For coumarin 153 bound to lysozyme, the average solvation time, hs s i is 330 ps. In the lysozyme-SDS complex, the solvation dynamics is markedly slower with hs s i ¼ 7250 ps. On addition of dithiothreitol (DTT) to the lysozyme-SDS complex, when the di-sulfide bonds are destroyed, hs s i is found to be 1140 ps. The slow dynamics in the denatured protein is attributed to the polymer chain dynamics and the exchange of bound and free water molecules.