Comparison of Acyl-Carrier Protein and Other Protein Structures in Aqueous Solutions by Fourier-Transform Infrared Spectroscopy
Document Type
Article
Publication Date
8-7-1993
Description
Protein solution structures were analyzed by horizontal attenuated total reflectance (ATR) FTIR spectroscopy. Secondary structure compositions determined from analyses of amide-I and II region and amide-III region difference spectra were compared. Data for proteins of known solution structure, cytochrome c, concanavalin A and lysozyme, were compared with those reported in the iiterature. Melittin, a peptide from bee venom whose secondary structural configuration varies depending upon solution conditions was also examined. Acyl-carrier protein (ACP) is a small protein of recognized dynamic structure that in its diverse physiologic roles interacts specifically with numerous different proteins. Horizontal ATR FTIR analysis of ACP's secondary structure indicated a predominately helical structure best defined as a combination of ordered and disordered helices. The FTIR-derived structural composition agreed with those determined for ACP by other techniques. Comparison of independent analyses of the amide-I and III regions to determine protein configuration compositions was a useful method of verifying the internal consistency of the calculated structural compositions of dynamically-structured proteins.
Citation Information
Ernst-Fonberg, Mary L.; Worsham, Lesa M.S.; and Williams, Sande G.. 1993. Comparison of Acyl-Carrier Protein and Other Protein Structures in Aqueous Solutions by Fourier-Transform Infrared Spectroscopy. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. Vol.1164(3). 273-282. https://doi.org/10.1016/0167-4838(93)90259-T PMID: 8343526 ISSN: 0167-4838