Gromiha M M, Ponnuswamy P K
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Int J Pept Protein Res. 1996 Nov;48(5):452-60. doi: 10.1111/j.1399-3011.1996.tb00863.x.
The analysis of known three-dimensional structures of membrane proteins provides an opportunity to understand their structure and stability. In this article we analyse the hydrophobic variation of amino acid residues at various ranges in membrane and aqueous parts of membrane proteins. The numerical indices for several properties of amino acid residues in membrane proteins, such as surrounding hydrophobicity, gain in surrounding hydrophobicity, hydrophobic gain ratio, accessible surface area, preference of amino acid residues in the interior and surface parts, solvent accessible reduction ratio and buriedness, were set up. The relative preference of amino acid residues at various positions of membrane proteins were obtained in a very realistic approach.
对膜蛋白已知三维结构的分析为理解其结构和稳定性提供了契机。在本文中，我们分析了膜蛋白的膜内部分和水相部分中不同区域氨基酸残基的疏水性变化。建立了膜蛋白中氨基酸残基若干性质的数值指标，如周围疏水性、周围疏水性增加量、疏水增加率、可及表面积、氨基酸残基在内部和表面部分的偏好性、溶剂可及性降低率和埋藏度。通过一种非常实际的方法得出了膜蛋白不同位置氨基酸残基的相对偏好性。
