Prediction and Fourier transform infrared spectroscopy estimation of the secondary structure of a Bacillus licheniformis endo-beta-1,3-1,4-D-glucanase.
The secondary structure of a recombinant Bacillus licheniformis endo-beta-1,3-1,4-D-glucanase (EC.3.2.1.73) has been estimated by Fourier Transform Infrared Spectroscopy and also predicted by the algorithm of Chou and Fasman. From the curve fitting of the deconvolved IR spectrum, the most probable distribution of the secondary structural classes appears to be about 40% beta-sheet, 25% reverse turn, 24% non-ordered and 11% alpha-helix. From theoretical prediction of secondary structure the protein would present 37% beta-sheet, 31% reverse turn, 22% non-ordered and 10% alpha-helix.
Querol
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E
Institut de Biologia Fonamental, Facultat de Ciencies, Universitat Autonoma de Barcelona, Spain.
Padrós
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E
Juncosa
M
M
Planas
A
A
Lloberas
J
J
D001407:Bacillus / Q000201:enzymology*; D005583:Fourier Analysis; D006026:Glycoside Hydrolases / Q000737:chemistry*; D008961:Models, Structural; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013055:Spectrophotometry, Infrared
D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; C028020:licheninase