Wolf E, Kim P S, Berger B
Howard Hughes Medical Institute, Whitehead Institute, MIT, Cambridge, Massachusetts 02142, USA.
Protein Sci. 1997 Jun;6(6):1179-89. doi: 10.1002/pro.5560060606.
A new multidimensional scoring approach for identifying and distinguishing trimeric and dimeric coiled coils is implemented in the MultiCoil program. The program extends the two-stranded coiled-coil prediction program PairCoil to the identification of three-stranded coiled coils. The computations are based upon data gathered from a three-stranded coiled-coil database comprising 6,319 amino acid residues, as well as from the previously constructed two-stranded coiled-coil database. In addition to identifying coiled coils not predicted by the two-stranded database programs, MultiCoil accurately classifies the oligomerization states of known dimeric and trimeric coiled coils. Analysis of the MultiCoil scores provides insight into structural features of coiled coils, and yields estimates that 0.9% of all protein residues form three-stranded coiled coils and that 1.5% form two-stranded coiled coils. The MultiCoil program is available at http:/(/)theory.lcs.mit.edu/multicoil.
一种用于识别和区分三聚体和二聚体卷曲螺旋的新的多维评分方法已在MultiCoil程序中实现。该程序将双链卷曲螺旋预测程序PairCoil扩展到三链卷曲螺旋的识别。计算基于从包含6319个氨基酸残基的三链卷曲螺旋数据库以及先前构建的双链卷曲螺旋数据库收集的数据。除了识别双链数据库程序未预测到的卷曲螺旋外,MultiCoil还能准确地对已知的二聚体和三聚体卷曲螺旋的寡聚化状态进行分类。对MultiCoil评分的分析有助于深入了解卷曲螺旋的结构特征,并得出估计值,即所有蛋白质残基中有0.9%形成三链卷曲螺旋,1.5%形成双链卷曲螺旋。MultiCoil程序可在http:/(/)theory.lcs.mit.edu/multicoil获取。