[Hydrogen-bond state analysis of cellobiohydrolase I molecule from Trichoderma viride].
Hydrogen-bond states on cellobiohydrolase II (CBH II) of Trichoderma viride were analysed by laser Raman spectroscopic method used to reveal molecular normal modes of vibration character. The results indicated that hydrogen-bond ability of carbonyl oxygen-atom of amide I was raised in two types of aqueous solution samples (6.0 and 8.0 of pH value) compared to the solid sample. The variation trend of beta structure modes was similar between amide II and amide I. As far as the ability of hydrogen-bond forming is concerned, tryptophan (Trp) and tyrosine (Typ) residues are strong hydrogen proton donor in pH 6.0 and solid sample, thus proving the results of previously spatial structure analysis. By analysis of free S-H character, the -S-S- construction in Trichoderma viride mature peptide has been proved to be the same as that of Trichoderma reesei.
Yu
Duo-wei
DW
Life Science College, Nanjing Normal University, Nanjing 210097, China.
Yuan
Sheng
S
D043366:Cellulose 1,4-beta-Cellobiosidase / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman / Q000379:methods*; D014242:Trichoderma / Q000201:enzymology*
D005656:Fungal Proteins; D043366:Cellulose 1,4-beta-Cellobiosidase