title: Detection of protein structure of frozen ancient human remains recovered from a glacier in Canada using synchrotron fourier transform infrared microspectroscopy.
abstract: We previously used synchrotron infrared microspectroscopy to describe the biochemical signature of skeletal muscle (biceps brachii) from the frozen ancient remains of a young man. In this current paper, we use light microscopy to assess the state of preservation of cellular components in the trapezius muscle from these same ancient remains and then use mid-infrared analysis at the Canadian Light Source synchrotron facility to further analyze the tissue. We compare spectra between the trapezius samples from the ancient remains and a recently deceased cadaver (control). Infrared spectra indicate preservation of secondary structure, with the α-helix being the principal component, along with triple helical portions of the protein backbone. Our mid-infrared analysis indicates an energy reserve in the skeletal muscle in the ancient remains.
authors: Paul Scherrer Institut, Villigen-PSI CH-5232, Switzerland.
authors: Luca
authors: L
authors: Quaroni
authors: Colleen R
authors: CR
authors: Christensen
authors: Becky
authors: B
authors: Chen
authors: Wayne
authors: W
authors: Vogl
authors: Maria Victoria
authors: MV
authors: Monsalve
mesh_terms: D002102:Cadaver; D002170:Canada; D005580:Fossils; D006801:Humans; D046448:Ice Cover; D009132:Muscles / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D011506:Proteins