Structural Characterization of Membrane Proteins and Peptides by FTIR and ATR-FTIR Spectroscopy

Fourier transform infrared spectroscopy is widely used in structural characterization of proteins or peptides

Suren A. Tatulian

2013

Scholarcy highlights

  • Fourier transform infrared spectroscopy is widely used in structural characterization of proteins or peptides
  • While the method does not have the capability of providing the precise, atomic-resolution molecular structure, it is exquisitely sensitive to conformational changes occurring in proteins upon functional transitions or upon intermolecular interactions
  • Sensitivity of vibrational frequencies to atomic masses has led to development of “isotope-edited” FTIR spectroscopy, where structural effects in two proteins, one unlabeled and the other labeled with a heavier stable isotope, such as 13C, are resolved simultaneously based on spectral downshift of the amide I band of the labeled protein
  • Negligible light scattering in the infrared region provides an opportunity to study intermolecular interactions between large protein complexes, interactions of proteins and peptides with lipid vesicles, or protein–nucleic acid interactions without light scattering problems often encountered in ultraviolet spectroscopy
  • Attenuated total reflection FTIR is a surface-sensitive version of infrared spectroscopy that has proved useful in studying membrane proteins and lipids, protein-membrane interactions, mechanisms of interfacial enzymes, and molecular architecture of membrane pore or channel forming proteins and peptides
  • Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data

Need more features? Save interactive summary cards to your Scholarcy Library.