Hopp T P
Torrey Pines Institute for Molecular Studies, San Diego, CA 92121.
Pept Res. 1993 Jul-Aug;6(4):183-90.
The Hopp and Woods hydrophilicity method for locating antigenic determinants was published in 1981. In the years since then, the method has been used widely and has played a vital role in many antigenic structure studies. The method has been criticized occasionally and replacements for it have been proposed. However, at this time, the Hopp and Woods method remains a method of choice for identifying antigenic sites and other protein interaction sites, because it has a higher success rate than other similar methods. Key to the success of this method is its cautious approach to charge-charge interactions, giving equal weight to positively and negatively charged residues, whereas other methods tend to favor one or the other. It has become clear that sites chosen by our method tend to be highly exposed, charged regions of the protein's surface which project into the environment and therefore have ample opportunity to contact other proteins. We have been exploring new uses for the method, and have found some applications in locating sites for other types of interactions, including those with other macromolecules such as DNA and RNA. It seems likely that this simple and reliable procedure will continue to find use in predicting the locations of major antigenic epitopes, and may also find use as a general prediction method to identify interaction sites on proteins that make charge-dependent contacts with a variety of other biological macromolecules.
霍普和伍兹用于定位抗原决定簇的亲水性方法于1981年发表。从那时起，该方法得到了广泛应用，并在许多抗原结构研究中发挥了至关重要的作用。该方法偶尔受到批评，也有人提出了替代方法。然而，目前霍普和伍兹方法仍然是识别抗原位点和其他蛋白质相互作用位点的首选方法，因为它比其他类似方法的成功率更高。该方法成功的关键在于其对电荷-电荷相互作用的谨慎处理方式，对带正电荷和带负电荷的残基给予同等权重，而其他方法往往更倾向于其中一种。很明显，我们的方法所选择的位点往往是蛋白质表面高度暴露的带电荷区域，这些区域伸向周围环境，因此有充分的机会与其他蛋白质接触。我们一直在探索该方法的新用途，并在定位与其他类型相互作用的位点方面发现了一些应用，包括与DNA和RNA等其他大分子的相互作用。这种简单可靠的程序似乎很可能会继续用于预测主要抗原表位的位置，也可能作为一种通用的预测方法，用于识别蛋白质上与各种其他生物大分子进行电荷依赖性接触的相互作用位点。
