Gromiha M M, Selvaraj S
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
J Biol Phys. 1997 Sep;23(3):151-62. doi: 10.1023/A:1004981409616.
An analysis of the dependence known three dimensional structure ofglobular proteins on their residue contacts and their interactions providesmuch information about their folding and stability. In this work, we analysethe residue-residue contacts and the role of medium and long rangeinteractions in globular proteins belonging to different structural classes.The results show that while medium range interactions predominate in allalpha class proteins, long range interactions predominate in all beta class.The residues Pro and Gly are found to have lowest medium range contacts,probably due to their helix breaking tendency. The hydrophobic residues Ile,Val and Tyr have higher long range contacts, and hence may serve as goodnucleation centres. Further, the role of charged residues and disulfidebridges in these interactions are also discussed.
对已知球状蛋白质三维结构对其残基接触及其相互作用的依赖性进行分析，可提供许多有关其折叠和稳定性的信息。在这项工作中，我们分析了不同结构类别的球状蛋白质中残基与残基的接触以及中远程相互作用的作用。结果表明，虽然中程相互作用在所有α类蛋白质中占主导地位，但远程相互作用在所有β类蛋白质中占主导地位。发现脯氨酸和甘氨酸残基的中程接触最少，这可能是由于它们的螺旋破坏倾向。疏水残基异亮氨酸、缬氨酸和酪氨酸具有较高的远程接触，因此可能是良好的成核中心。此外，还讨论了带电荷残基和二硫键在这些相互作用中的作用。
