HYDROPHOBICITY OF AMINO-ACID RESIDUES IN GLOBULAR-PROTEINS
HYDROPHOBICITY OF AMINO-ACID RESIDUES IN GLOBULAR-PROTEINS
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DOI：
10.1126/science.4023714
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发表时间：
1985-01-01
期刊：
影响因子：
56.9
通讯作者：
ZEHFUS, MH
中科院分区：
文献类型：
--
作者：
ROSE, GD;GESELOWITZ, AR;ZEHFUS, MH
在生物合成过程中，球状蛋白质折叠成紧密的颗粒，其内部核心与周围的溶剂隔离。疏水效应被认为在介导这一过程中发挥着关键作用：从水中排出的非极性残留物产生了可以将它们埋藏的分子内部。矛盾的是，早期定量分析的结果表明，非极性残基埋藏在蛋白质内的趋势很弱。然而，此类分析仅将残留物分类为“暴露”或“掩埋”。在本文报道的实验中，已知结构的蛋白质被用来测量每个残基在折叠时埋藏的平均面积。该特征量，即埋藏的平均面积，与残留物的疏水性相关。
During biosynthesis, a globular protein folds into a tight particle with an interior core that is shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in mediating this process: nonpolar residues expelled from water engender a molecular interior where they can be buried. Paradoxically, results of earlier quantitative analyses have suggested that the tendency for nonpolar residues to be buried within proteins is weak. However, such analyses merely classify residues as either "exposed" or "buried." In the experiment reported in this article proteins of known structure were used to measure the average area that each residue buries upon folding. This characteristic quantity, the average area buried, is correlated with residue hydrophobicity.