Laser-excited Raman spectroscopy of biomolecules: II. Native ribonuclease and α-chymotrypsin☆☆☆

摘要: Laser-excited Raman spectra of native ribonuclease and α-chymotrypsin the polypeptide poly-l-glutamic acid have been determined in aqueous solution. With help previously quantitative amino acids, a considerable portion spectral details has interpreted. The strong lines due to aromatic side chains amino-acid residues are clearly observed not affected by conformations proteins. bond-stretching vibration disulfide link shows up strongly spectrum at measurably different position (516 cm−1) from its location lysozyme (509 cm−1). intensity ratio C-S S-S is an order magnitude larger than lysozyme. Both these observations suggest that C-S-S-C cross-links two proteins significantly different. pH 10 was as possible model for effects denaturation. While denatured yet obtained, comparison with latter expected broadening overlapping peaks amide I III regions which sharper resolved into several components protein spectra.