Kim Changsik, Choi Jiwon, Lee Seong Joon, Welsh William J, Yoon Sukjoon
Sookmyung Women's University, Department of Biological Sciences, Hyochangwon-gil 52, Yongsan-gu, Seoul, Republic of Korea.
Nucleic Acids Res. 2009 Jul;37(Web Server issue):W469-73. doi: 10.1093/nar/gkp351. Epub 2009 May 25.
The calculation of contact-dependent secondary structure propensity (CSSP) is a unique and sensitive method that detects non-native secondary structure propensities in protein sequences. This method has applications in predicting local conformational change, which typically is observed in core sequences of protein aggregation and amyloid fibril formation. NetCSSP implements the latest version of the CSSP algorithm and provides a Flash chart-based graphic interface that enables an interactive calculation of CSSP values for any user-selected regions in a given protein sequence. This feature also can quantitatively estimate the mutational effect on changes in native or non-native secondary structural propensities in local sequences. In addition, this web tool provides precalculated non-native secondary structure propensities for over 1,400,000 fragments that are seven-residues long, collected from PDB structures. They are searchable for chameleon subsequences that can serve as the core of amyloid fibril formation. The NetCSSP web tool is available at http://cssp2.sookmyung.ac.kr/.
接触依赖性二级结构倾向(CSSP)的计算是一种独特且灵敏的方法,可检测蛋白质序列中的非天然二级结构倾向。该方法可用于预测局部构象变化,这种变化通常在蛋白质聚集和淀粉样原纤维形成的核心序列中观察到。NetCSSP实现了CSSP算法的最新版本,并提供了基于Flash图表的图形界面,能够对给定蛋白质序列中任何用户选择的区域进行CSSP值的交互式计算。此功能还可以定量估计突变对局部序列中天然或非天然二级结构倾向变化的影响。此外,该网络工具提供了从PDB结构中收集的超过140万个七个残基长的片段的预先计算的非天然二级结构倾向。它们可用于搜索可作为淀粉样原纤维形成核心的变色龙子序列。NetCSSP网络工具可在http://cssp2.sookmyung.ac.kr/获取。