Is X-ray absorption spectroscopy sensitive to the amino acid composition of functional proteins?

J Phys Chem B. 2008 Apr 17;112(15):4478-80. doi: 10.1021/jp801248n. Epub 2008 Mar 22.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Animals
  • Cattle
  • Collagen Type I / chemistry*
  • Muramidase / chemistry*
  • Ovalbumin / chemistry*
  • Sensitivity and Specificity
  • Serum Albumin, Bovine / chemistry*
  • Spectrum Analysis / methods*
  • X-Rays

Substances

  • Amino Acids
  • Collagen Type I
  • Serum Albumin, Bovine
  • Ovalbumin
  • Muramidase