title: Is X-ray absorption spectroscopy sensitive to the amino acid composition of functional proteins?
abstract: We report, compare, and analyze near-edge X-ray absorption fine structure (NEXAFS) spectra of powder samples of four different functional proteins, namely, lysozyme, ovalbumin, bovine serum albumin, and type-I collagen, at all relevant absorption edges. The spectra of all of the above proteins were found to be quite similar and to exhibit minor differences only. Nevertheless, despite the general similarity, the spectra of the individual proteins are distinguishable, and some of the respective differences clearly correlate with their amino acid compositions. Further factors affecting the NEXAFS spectra of proteins beyond the building block approach are discussed.
authors: Angewandte Physikalische Chemie, University of Heidelberg, INF 253, 69120 Heidelberg, Germany. yan.zubavichus@urz.uniheidelberg.de
authors: Yan
authors: Y
authors: Zubavichus
authors: Andrey
authors: A
authors: Shaporenko
authors: Michael
authors: M
authors: Grunze
authors: Michael
authors: M
authors: Zharnikov
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D010047:Ovalbumin / Q000737:chemistry*; D012680:Sensitivity and Specificity; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods*; D014965:X-Rays
chemical_list: D000596:Amino Acids; D024042:Collagen Type I; D012710:Serum Albumin, Bovine; D010047:Ovalbumin; D009113:Muramidase