Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlations in Fourier transform infrared spectroscopy.
Fourier transform infrared spectroscopy has become well known as a sensitive and informative tool for studying secondary structure in proteins. Present analysis of the conformation-sensitive amide I region in protein infrared spectra, when combined with band narrowing techniques, provides more information concerning protein secondary structure than can be meaningfully interpreted. This is due in part to limited models for secondary structure. Using the algorithm described in the previous paper of this series, we have generated a library of substructures for several trypsin-like serine proteases. This library was used as a basis for spectra-structure correlations with infrared spectra in the amide I' region, for five homologous proteins for which spectra were collected. Use of the substructure library has allowed correlations not previously possible with template-based methods of protein conformational analysis.
Prestrelski
S J
SJ
Department of Physiology and Biophysics, Mount Sinai School of Medicine of the City University of New York, New York 10029.
Byler
D M
DM
Liebman
M N
MN
D000465:Algorithms; D000577:Amides / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D016208:Databases, Factual; D005583:Fourier Analysis; D017433:Protein Structure, Secondary; D012697:Serine Endopeptidases / Q000737:chemistry*; D013055:Spectrophotometry, Infrared; D013552:Swine
D000577:Amides; D012697:Serine Endopeptidases