The results showed that the thiobarbituric acid value ( tba ) decreased while the protein oxidation value and the surface hydrophobicity increased with a red shift of maximum emission wavelength ; the changes of protein secondary structure were obvious .
We get different result when using different physical character to classify the amino acids and then relate it with the chemical bonds and physical effect which can stabilize protein . We find the hydrophobicity and hydrophilicity may be more important to structural symmetry .
The hydrophobicity is related to molecular volume and polarity .
分子的疏水性跟分子的体积和极性有关。
The mixture of hydrophobicity and hydrophilicity in each novel protein means that the resulting materials are often different when different solvents are used , even though the underlying proteins are the same .