Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy

Michael T. Ruggiero, Juraj Sibik, Roberto Orlando, J. Axel Zeitler, Timothy Michael Korter

Research output: Contribution to journalArticle

25 Scopus citations


The rigidity of poly-l-proline is an important contributor to the stability of many protein secondary structures, where it has been shown to strongly influence bulk flexibility. The experimental Young's moduli of two known poly-l-proline helical forms, right-handed all-cis (FormI) and left-handed all-trans (FormII), were determined in the crystalline state by using an approach that combines terahertz time-domain spectroscopy, X-ray diffraction, and solid-state density functional theory. Contrary to expectations, the helices were found to be considerably less rigid than many other natural and synthetic polymers, as well as differing greatly from each other, with Young's moduli of 4.9 and 9.6GPa for FormsI and II, respectively.

Original languageEnglish (US)
JournalAngewandte Chemie - International Edition
StateAccepted/In press - 2016


  • Biopolymers
  • Elasticity
  • Polyproline
  • Proteins
  • Terahertz spectroscopy

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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