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Structural dynamics of cisplatin binding to histidine in a protein
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/content/aip/journal/sdy/1/3/10.1063/1.4883975
2014-06-17
2014-09-16

Abstract

The platinum anti-cancer agents cisplatin and carboplatin bind to the histidine 15 residue in the model protein hen egg white lysozyme. By using temperatures either side of the protein glass transition state (∼180 K), several platinum binding modes are seen and show that not all these platinum modes are stable. In particular, the mean square displacement vibration amplitudes of the cisplatin and of the histidine to which it is bound are analysed in detail. As well as the multiple platinum peaks, the electron density for the His-15 side chain is weak to absent at 150 K and 200 K, which points to the imidazole ring of the His side chain sampling multiple positions. Most interestingly, the His-15 imidazole becomes more ordered at room temperature.

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Scitation: Structural dynamics of cisplatin binding to histidine in a protein
http://aip.metastore.ingenta.com/content/aip/journal/sdy/1/3/10.1063/1.4883975
10.1063/1.4883975
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