光谱实验室
光譜實驗室
광보실험실
CHINESE JOURNAL OF SPECTROSCOPY LABORATORY
2010年
1期
102-106
,共5页
傅里叶变换红外光谱%蛋白质%二级结构
傅裏葉變換紅外光譜%蛋白質%二級結構
부리협변환홍외광보%단백질%이급결구
Fourier Transformation Infrared Spectroscopy%Protein%Secondary Structure
通过FTIR光学信息研究液态和固态磷脂酶D的二级结构.结果表明FTIR光学信息是一种有效的蛋白质分子二级结构研究方法.FTIR的光学信息分析表明冻干胁迫下,磷脂酶D的FTlR光学信息及二级结构发生较大变化.在磷脂酶D活性构象时的pH冻干使磷脂酶Dα螺旋大大下降.无规卷曲大大上升,β折叠几乎没有变化,说明PLD蛋白质分子空间有序构象解体严重.功能性试验表明,磷脂酶D二级结构的变化直接导致了其活性发生很大变化.
通過FTIR光學信息研究液態和固態燐脂酶D的二級結構.結果錶明FTIR光學信息是一種有效的蛋白質分子二級結構研究方法.FTIR的光學信息分析錶明凍榦脅迫下,燐脂酶D的FTlR光學信息及二級結構髮生較大變化.在燐脂酶D活性構象時的pH凍榦使燐脂酶Dα螺鏇大大下降.無規捲麯大大上升,β摺疊幾乎沒有變化,說明PLD蛋白質分子空間有序構象解體嚴重.功能性試驗錶明,燐脂酶D二級結構的變化直接導緻瞭其活性髮生很大變化.
통과FTIR광학신식연구액태화고태린지매D적이급결구.결과표명FTIR광학신식시일충유효적단백질분자이급결구연구방법.FTIR적광학신식분석표명동간협박하,린지매D적FTlR광학신식급이급결구발생교대변화.재린지매D활성구상시적pH동간사린지매Dα라선대대하강.무규권곡대대상승,β절첩궤호몰유변화,설명PLD단백질분자공간유서구상해체엄중.공능성시험표명,린지매D이급결구적변화직접도치료기활성발생흔대변화.
The liquid and solid PLD secondary structure were characterized by optical information of FTIR.The results showed that optical information of FTIR was an effective method for researching protein secondary structure.The optical information of FTIR shows that α-helix of PLD is greatly decreased,random coil of PLD is greatly increased and β-sheet of PLD almost is no change under freeze-dried duress when PLD is processed by freeze-drying under the condition of PLD active conformation pH.That suggested PLD protein conformational space in an orderly were disjointed seriously.The functional test show that the secondary structure change PLD is related with he activity of PLD.