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Detection of Protein Structure of Frozen Ancient Human Remains Recovered from a Glacier in Canada Using Synchrotron Fourier Transform Infrared Microspectroscopy

Published online by Cambridge University Press:  07 May 2013

Luca Quaroni
Affiliation:
Paul Scherrer Institut, Villigen-PSI CH-5232, Switzerland
Colleen R. Christensen
Affiliation:
College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK, CanadaS7N 5A8
Becky Chen
Affiliation:
Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC, CanadaV6T 1Z3
Wayne Vogl
Affiliation:
Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, CanadaV6T 1Z3
Maria Victoria Monsalve*
Affiliation:
Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC, CanadaV6T 1Z3
*
*Corresponding author. E-mail: vmonsalve@pathology.ubc.ca
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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.

Type
Biological Applications
Copyright
Copyright © Microscopy Society of America 2013 

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