Spectroscopic studies reveal conformational flexibility of intrinsically unstructured protein HYPK

• 作 者: Swasti Raychaudhuri Kamalika R
• 机 构: 不详
• 出 处: 生物物理化学(英文)
• 发表日期: 2011年4期
• 关键词: IUP HUNTINGTIN Yeast-Two Hybrid Protein K TYROSINE Fluorescence Conformational C

The chaperone-like huntingtin-interacting protein, HYPK, has unusual biophysical behavior like an intrinsically unstructured protein (IUP). The protein exists as a (pre-) molten globule with ~37% residual structure and shows com- paction in presence of Ca