The Synchrotron Radiation Circular Dichroism (SRCD) and the estimation of secondary structure of Proteins

• Main Authors: Card Kao, 高晨
• Other Authors: Wei-Ning Huang
• Format: Others
• Language: zh-TW
• Online Access: http://ndltd.ncl.edu.tw/handle/wb7336

碩士 === 元培科技大學 === 生物技術研究所 === 102 === Circular dichroism (CD) is an absorption difference spectrum of left and right circularly polarized light. Traditional circular dichroism unable to detect the vacuum ultraviolet spectra because the light source limiting.Synchrotron radiation circular dichroism (SRCD) can measure the extending wavelength to vacuum ultraviolet range. CD spectra can estimate the proportion ofprotein secondary structure effectively. We developed a newprogram,CD_Fit5, which estimates protein secondary structure, it first searchsand matchs a CD spectrum froma data setby NRMSD criterion. Secondly, the residued spectra of subtractedqueryspectrum by match protein was constructed by linear combination of 4 peptides of 100% secondary structure of helix, beta, turn and coil. Finally, take the sum of these two results to estimate the proportion of protein secondary structure . For CD_Fit5optimizeddatasets, we use the SRCD collect many CD spectra of standard peptide/proteins in some special conditions and we alsocompared a few published computing program, such as SELCON3, CDSSTR so on. It showed that the estimation of protein secondary structure by optimizing dataset of CD_Fit5 have similar results as published programs, even closer to the actual value.