Molten-Globule of Proteins and Its Physiological Role

熔球为致密变性态，二级结构较多，三级结构无序较多。为了了解熔融球在蛋白质折叠中的作用及其生理作用，我们研究了各种蛋白质的熔融球的构象和稳定性以及肽的相应状态。我们得到了以下主要结果：熔融球的稳定性是由各种力的平衡决定的。我们发现静电斥力是破坏熔融球状态稳定的关键因素。用小角x射线散射研究了细胞色素c的熔融球，并对其构象性质进行了研究。我们发现细胞色素c在生理条件下（即中性ph、生理温度和无变性剂）的可逆变性构象是熔融的球状体。我们展示了蜂毒素和两亲性多肽的阴离子和ph依赖性构象转变的机制。我们发现，胍-盐酸盐诱导酸未折叠蛋白的再折叠，稳定熔融球状态。

The molten globule is a compact denatured state with a significant amount of secondary structure, but largely disordered tertiary structure. To understand the role of the molten globule in protein folding and its physiological role, we studied the conformation and stability of the molten globule of various proteins and the corresponding state of peptides. We obtained following major results.1. The stability of the molten globule is determined by a balance of various forces. We showed that electrostatic repulsion is a critical factor destabilizing the molten globule state.2. The molten globule of cytochrome c was studied by small angle X-ray scattering and its conformational properties were clarified.3. We indicated that the reversibly denatured conformation of cytochrome c under physiological conditions (i.e. neutral ph, physiological temperature and no denaturant) is the molten globule.4. We showed the mechanism of the anion and ph-dependent conformational transition of melittin and an amphiphilic polypeptide.5. We showed that Guanidine-Hydrochloride induces the refolding of acid-unfolded proteins, stabilizing the molten globule state.