The regression model for octanol/water partition coefficients ( K ow ), is founded with only two molecular descriptors available through quantum chemical calculations: solvation free energy (Δ G S ), and so...The regression model for octanol/water partition coefficients ( K ow ), is founded with only two molecular descriptors available through quantum chemical calculations: solvation free energy (Δ G S ), and solvent accessible surface area (SASA). For the properties of 47 organic compounds from 17 types, the model gives a correction coefficient (adjusted for degrees of freedom) of 0 959 and a standard error of 0 277 log unit. It is a suitable way to predict the partition properties that are related to solute solvent interactions in the water phase.展开更多
It is well known that the SEA-TROSY experiment could alleviate some of the problems of resonance overlap in 15N/2H labeled proteins as it was designed to selectively map solvent exposed amide protons. However, SEA- TR...It is well known that the SEA-TROSY experiment could alleviate some of the problems of resonance overlap in 15N/2H labeled proteins as it was designed to selectively map solvent exposed amide protons. However, SEA- TROSY spectra may be contaminated with exchange-relayed NOE contributions from fast exchanged hydroxyl or amine protons and contributions from longitudinal relaxation. Also, perdeuteration of the protein sample is a pre-requisite for this experiment. In this communication, a modified version, clean SEA-TROSY, was proposed to eliminate these artifacts and to allow the experiment to be applied to protonated or partially deuterated proteins and protein complexes.展开更多
The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b 5 are located at the edge of the heme binding pocket. The solvent accessible areas of the “pocket interior” of the four mutants ...The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b 5 are located at the edge of the heme binding pocket. The solvent accessible areas of the “pocket interior” of the four mutants and the wild type cytochrome b 5 have been calculated based on their crystal structures at high resolution. The change in the hydrophobicity of the heme binding pocket resulting from the mutation can be quantitatively described using the difference of the solvent accessible area of the “pocket interior” of each mutant from that of the wild type cytochrome b 5. The influences of the hydrophobicity of the heme binding pocket on the protein stability and redox potential are discussed.展开更多
基金TheNationalNaturalScienceFoundationofChina (No .2 9837180 )andtheResearchFoundationfortheDoctoralProgramofHigherEducationofChi
文摘The regression model for octanol/water partition coefficients ( K ow ), is founded with only two molecular descriptors available through quantum chemical calculations: solvation free energy (Δ G S ), and solvent accessible surface area (SASA). For the properties of 47 organic compounds from 17 types, the model gives a correction coefficient (adjusted for degrees of freedom) of 0 959 and a standard error of 0 277 log unit. It is a suitable way to predict the partition properties that are related to solute solvent interactions in the water phase.
基金Project supported by the grants from One Hundred Talent Program of the Chinese Academy of Sciences and Shanghai Commission of Science and Technology (No. 03JC14081).
文摘It is well known that the SEA-TROSY experiment could alleviate some of the problems of resonance overlap in 15N/2H labeled proteins as it was designed to selectively map solvent exposed amide protons. However, SEA- TROSY spectra may be contaminated with exchange-relayed NOE contributions from fast exchanged hydroxyl or amine protons and contributions from longitudinal relaxation. Also, perdeuteration of the protein sample is a pre-requisite for this experiment. In this communication, a modified version, clean SEA-TROSY, was proposed to eliminate these artifacts and to allow the experiment to be applied to protonated or partially deuterated proteins and protein complexes.
文摘The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b 5 are located at the edge of the heme binding pocket. The solvent accessible areas of the “pocket interior” of the four mutants and the wild type cytochrome b 5 have been calculated based on their crystal structures at high resolution. The change in the hydrophobicity of the heme binding pocket resulting from the mutation can be quantitatively described using the difference of the solvent accessible area of the “pocket interior” of each mutant from that of the wild type cytochrome b 5. The influences of the hydrophobicity of the heme binding pocket on the protein stability and redox potential are discussed.
