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首页> 外文会议>Pacific Symposium on Biocomputing 2001, Jan 3-7, 2001, Mauna Lani, Hawaii >THE PROTEIN NON-FOLDING PROBLEM: AMINO ACID DETERMINANTS OF INTRINSIC ORDER AND DISORDER
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THE PROTEIN NON-FOLDING PROBLEM: AMINO ACID DETERMINANTS OF INTRINSIC ORDER AND DISORDER

机译：蛋白质非折叠问题：内在有序和无序的氨基酸决定因素

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摘要

To investigate the determinants of protein order and disorder, three primary and one derivative database of intrinsically disordered proteins were compiled. The segments in each primary database were characterized by one of the following: X-ray crystallography, nuclear magnetic resonance (NMR), or circular dichroism (CD). The derivative database was based on homology. The three primary disordered databases have a combined total of 157 proteins or segments of length * 30 with 18,010 residues, while the derivative database contains 572 proteins from 32 families with 52,688 putatively disordered residues. For the four disordered databases, the amino acid compositions were compared with those from a database of ordered structure. Relative to the ordered protein, the intrinsically disordered segments in all four databases were significantly depleted in W, C, F, I, Y, V, L and N, significantly enriched in A, R, G, Q, S, P, E and K, and inconsistently different in H, M, T, and D, suggesting that the first set be called order-promoting and the second set disorder-promoting. Also, 265 amino acid properties were ranked by their ability to discriminate order and disorder and then pruned to remove the most highly correlated pairs. The 10 highest-ranking properties after pruning consisted of 2 residue contact scales, 4 hydrophobicity scales, 3 scales associated with *-sheets and one polarity scale. Using these 10 properties for comparisons of the 3 primary databases suggests that disorder in all 3 databases is very similar, but with those characterized by NMR and CD being the most similar, those by CD and X-ray being next, and those by NMR and X-ray being the least similar.
机译：为了研究决定蛋白质顺序和紊乱的因素，编制了三个主要的和一个固有的紊乱蛋白质的衍生数据库。每个主要数据库中的片段通过以下特征之一进行表征：X射线晶体学，核磁共振（NMR）或圆二色性（CD）。派生数据库基于同源性。三个主要的无序数据库总共包含157个蛋白质或长度* 30的片段，具有18,010个残基，而衍生数据库包含来自32个科的572个蛋白质，具有52,688个可能的无序残基。对于四个无序数据库，将氨基酸组成与有序结构数据库中的氨基酸组成进行了比较。相对于有序蛋白质，所有四个数据库中的内在无序节段中的W，C，F，I，Y，V，L和N均显着耗尽，而A，R，G，Q，S，P，E则显着富集和K，并且在H，M，T和D方面不一致，这表明第一组被称为促进顺序，第二组被称为促进混乱。另外，对265个氨基酸的特性进行了区分顺序和无序能力的排名，然后对其进行修剪以去除相关性最高的对。修剪后的10个最高等级属性包括2个残留物接触标度，4个疏水性标度，3个与* -sheets相关的标度和一个极性标度。使用这10个属性进行3个主要数据库的比较表明，所有3个数据库中的无序情况非常相似，但以NMR和CD为特征的异常最为相似，以CD和X射线为第二的特征，其次为NMR和CD X射线最不相似。

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