Author
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DUKOR, RINA - BIOINFORMATICS/VYSIS,INC |
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LIEBMAN, MICHAEL - BIOINFORMATICS/VYSIS, INC |
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NABETANI, HIROSHI - NATIONAL FOOD RES INST |
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Abbott Dr, Thomas |
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Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 6/19/1996 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Protein secondary structure in solution is generally believed to be essentially similar to the structure in crystalline state in spite of limited examples to the contrary. X-ray diffraction studies of protein crystals have been the standard to which other structural analyses are compared and thus it is important to quantitatively assess protein conformation in the two states. FTIR spectroscopy and microspectroscopy were used to compare the structure of nine proteins in solution, solid and crystalline states. Four of the nine proteins plus elastase (studied in solution only) represent an homologous set of serine proteases, whose structures are closely related. In addition, two proteins represent zymogen activation where the structural differences between zymogen and the active enzyme are small. The set was chosen to establish a baseline for detection of small differences by FTIR spectroscopy. First, the difference FTIR crystal spectrum (absorbance or second derivative) between two proteins such as zymogen and active enzyme is computed and analyzed by comparison to a Difference Linear Distance (LD) analysis of crystallographic data to enhance interpretation of the observed peaks. Once this baseline is established, the solution and crystal spectra are compared for the other proteins. For all proteins studied, the amide I absorbance band was broader in the crystalline protein spectra compared to the spectra in solution and only the spectrum of papain crystals appears to exhibit differences from the solution spectrum. |
