期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 121, 期 40, 页码 9336-9347出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b07032
关键词
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资金
- DST-SERB [ECR/2015/000027]
- CSIR-National Chemical Laboratory [CSC 0134]
- CSIR-National Chemical Laboratory (MLP) [030026]
- University Grants Commission, India
It has been difficult to quantify the degree of side-chain conformational heterogeneity in the native (N) state ensemble of proteins and the relative energetic contributions of the side-chain packing and the hydrophobic effect in protein stability. Here, we show using multiple site specific spectroscopic probes and tools of thermodynamics that the N state ensemble of a multidomain protein contains an equilibrium intermediate (I) whose interdomain region resembles a dry molten globule. In the I state, a tryptophan residue in the interdomain region is alternatively packed, but its secondary structure and intradomain packing are N-like. The I state also has a larger interdomain distance, but the domain-domain interface is dry and molten. Our results indicate that hydrophobic desolvation and side-chain packing are decoupled during protein folding and that interdomain packing interactions have an important energetic contribution in protein stability. Dynamic interconversion between alternatively packed N-like states could be important for multiple allosteric and ligand binding functions of this protein.
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