title: Using enzyme folding to explore the mechanism of therapeutic touch: a feasibility study.
abstract: OBJECTIVE
  The goal of this research is to design a novel model using protein folding to study Therapeutic Touch, a noncontact form of energy manipulation healing. Presented is a feasibility study suggesting that the denaturation path of ribonuclease A may be a useful model to study the energy exchange underlying therapeutic touch.
  
  
  METHODS
  The folding of ribonuclease A serves as a controlled energy-requiring system in which energy manipulation can be measured by the degree of folding achieved. A kinetic assay and fluorescence spectroscopy are used to assess the enzyme-folding state.
  
  
  RESULTS
  The data suggest that the kinetic assay is a useful means of assessing the degree of refolding, and specifically, the enzyme function. However, fluorescence spectroscopy was not shown to be an effective measurement of enzyme structure for the purposes of this work.
  
  
  CONCLUSIONS
  More research is needed to assess the underlying mechanism of therapeutic touch to complement the existing studies. An enzyme-folding model may provide a useful means of studying the energy exchange in therapeutic touch.
authors.affiliation: Drexel University College of Medicine, Philadelphia, PA, USA.
authors.forename: Mallory L
authors.initials: ML
authors.lastname: Strickland
authors.forename: Helen M
authors.initials: HM
authors.lastname: Boylan
mesh_terms: D000818:Animals; D002417:Cattle; D005240:Feasibility Studies; D008958:Models, Molecular; D017510:Protein Folding; D020673:Protein Renaturation; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000378:metabolism; D019124:Therapeutic Touch
chemical_list: D012259:Ribonuclease, Pancreatic