Share Email Print
cover

Proceedings Paper

Effect of structural modification on second harmonic generation in collagen
Format Member Price Non-Member Price
PDF $14.40 $18.00

Paper Abstract

The effects of structural perturbation on second harmonic generation in collagen were investigated. Type I collagen fascicles obtained from rat tails were structurally modified by increasing nonenzymatic cross-linking, by thermal denaturation, by collagenase digestion, or by dehydration. Changes in polarization dependence were observed in the dehydrated samples. Surprisingly, no changes in polarization dependence were observed in highly crosslinked samples, despite significant alterations in packing structure. Complete thermal denaturation and collagenase digestion produced samples with no detectable second harmonic signal. Prior to loss of signal, no change in polarization dependence was observed in partially heated or digested collagen.

Paper Details

Date Published: 10 July 2003
PDF: 11 pages
Proc. SPIE 4963, Multiphoton Microscopy in the Biomedical Sciences III, (10 July 2003); doi: 10.1117/12.477998
Show Author Affiliations
Patrick Christian Stoller, Lawrence Livermore National Lab. (United States)
Karen M. Reiser, Univ. of California/Davis (United States)
Peter M. Celliers, Lawrence Livermore National Lab. (United States)
Alexander M. Rubenchik, Lawrence Livermore National Lab. (United States)


Published in SPIE Proceedings Vol. 4963:
Multiphoton Microscopy in the Biomedical Sciences III
Ammasi Periasamy; Peter T. C. So, Editor(s)

© SPIE. Terms of Use
Back to Top