Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif

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• 作者：Danyun Zeng ; Qingliang Shen ; Jae-Hyun Cho ; ^{jaehyuncho@tamu.edu}
• 关键词：Intrinsically disordered proteins ; Conformational entropy ; SH3 domain ; Proline-rich motif ; Protein-protein interactions
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：26 February 2017
• 年：2017
• 卷：484
• 期：1
• 页码：21-26
• 全文大小：802 K
• 卷排序：484

文摘

Conformational entropy plays critical roles in the regulation of protein-protein interactions. Conformational entropy change upon binding of disordered ligands to a protein is not well understood. We estimated backbone conformational entropy change upon complexation of SH3 domain and PRM. Energetic contribution of backbone conformational entropy is significant in SH3-PRM interaction.