Thermodynamic hypothesis and kinetic stabil- ity are currently used to understand protein folding. The former assumes that free energy minimum is the exclusive dominant mechanism in most cases, while the latter shows ...Thermodynamic hypothesis and kinetic stabil- ity are currently used to understand protein folding. The former assumes that free energy minimum is the exclusive dominant mechanism in most cases, while the latter shows that some proteins have even lower free energy in inter- mediate states and their native states are kinetically trapped in the higher free energy region. This article explores the stability condition of protein structures on the basis of our study of complex chemical systems. We believe that sep- arating one from another is not reasonable since they should be coupled, and protein structures should be dom- inated by at least two mechanisms resulting in different characteristic states. It is concluded that: (1) Structures of proteins are dynamic, showing multiple characteristic states emerging alternately and each dominated by a respective mechanism. (2) Compromise in competition of multiple dominant mechanisms might be the key to understanding the stability of protein structures. (3) The dynamic process of protein folding should be depicted through the time series of both its energetic and structural changes, which is much meaningful and applicable than the free energy landscape.展开更多
A high strength Mg-5.1Zn-3.2Y-0.4Zr-0.4Ca (wt%) alloy containing W phase (Mg3Y2Zn3) prepared by permanent mold direct-chill casting is indirectly extruded at 350 ℃ and 400 ℃, respectively. The extruded alloys sh...A high strength Mg-5.1Zn-3.2Y-0.4Zr-0.4Ca (wt%) alloy containing W phase (Mg3Y2Zn3) prepared by permanent mold direct-chill casting is indirectly extruded at 350 ℃ and 400 ℃, respectively. The extruded alloys show bimodal grain structure consisting of fine dynamic recrystallized (DRXed) grains and unre- crystallized coarse regions containing fine W phase and β2′ precipitates. The fragmented W phase particles induced by extrusion stimulate nucleation of DRXed grains, leading to the formation of fine DRXed grains, which are mainly distributed near the W particle bands along the extrusion direction. The alloy extruded at 350 ℃ exhibits yield strength of 373 MPa, ultimate tensile strength of 403 MPa and elongation to failure of 5.1%. While the alloy extruded at 400 ℃ shows lower yield strength of 332 MPa, ultimate tensile strength of 352 MPa and higher elongation to failure of 12%. The mechanical properties of the as-extruded alloys vary with the distribution and size of W phase. A higher fraction of DRXed grains is obtained due to the homogeneous distribution of micron-scale broken W phase particles in the alloy extruded at 400 ℃, which can lead to higher ductility. In addition, the nano-scale dynamic W phase precipitates distributed in the unDRXed regions are refined at lower extrusion temperature. The smaller size of nano-scale W phase precipitates leads to a higher fraction of unDRXed regions which contributes to higher strength of the alloy extruded at 350 ℃.展开更多
基金supported by the National Natural Science Foundation of China(21103195)the Knowledge Innovation Program of Chinese Academy of Sciences(KGCX2-YW-124)
文摘Thermodynamic hypothesis and kinetic stabil- ity are currently used to understand protein folding. The former assumes that free energy minimum is the exclusive dominant mechanism in most cases, while the latter shows that some proteins have even lower free energy in inter- mediate states and their native states are kinetically trapped in the higher free energy region. This article explores the stability condition of protein structures on the basis of our study of complex chemical systems. We believe that sep- arating one from another is not reasonable since they should be coupled, and protein structures should be dom- inated by at least two mechanisms resulting in different characteristic states. It is concluded that: (1) Structures of proteins are dynamic, showing multiple characteristic states emerging alternately and each dominated by a respective mechanism. (2) Compromise in competition of multiple dominant mechanisms might be the key to understanding the stability of protein structures. (3) The dynamic process of protein folding should be depicted through the time series of both its energetic and structural changes, which is much meaningful and applicable than the free energy landscape.
基金supported financially by the National Key Research and Development Program of China (No. 2016YFB0301102)the National Natural Science Foundation of China (No. 51571068)
文摘A high strength Mg-5.1Zn-3.2Y-0.4Zr-0.4Ca (wt%) alloy containing W phase (Mg3Y2Zn3) prepared by permanent mold direct-chill casting is indirectly extruded at 350 ℃ and 400 ℃, respectively. The extruded alloys show bimodal grain structure consisting of fine dynamic recrystallized (DRXed) grains and unre- crystallized coarse regions containing fine W phase and β2′ precipitates. The fragmented W phase particles induced by extrusion stimulate nucleation of DRXed grains, leading to the formation of fine DRXed grains, which are mainly distributed near the W particle bands along the extrusion direction. The alloy extruded at 350 ℃ exhibits yield strength of 373 MPa, ultimate tensile strength of 403 MPa and elongation to failure of 5.1%. While the alloy extruded at 400 ℃ shows lower yield strength of 332 MPa, ultimate tensile strength of 352 MPa and higher elongation to failure of 12%. The mechanical properties of the as-extruded alloys vary with the distribution and size of W phase. A higher fraction of DRXed grains is obtained due to the homogeneous distribution of micron-scale broken W phase particles in the alloy extruded at 400 ℃, which can lead to higher ductility. In addition, the nano-scale dynamic W phase precipitates distributed in the unDRXed regions are refined at lower extrusion temperature. The smaller size of nano-scale W phase precipitates leads to a higher fraction of unDRXed regions which contributes to higher strength of the alloy extruded at 350 ℃.