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

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

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

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 (Form I) and left-handed all-trans (Form II), 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 9.6 GPa for Forms I and II, respectively. Spring fever: The experimental Young's moduli of two known poly-L-proline helical forms 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.

Original languageEnglish (US)
Pages (from-to)6877-6881
Number of pages5
JournalAngewandte Chemie - International Edition
Volume55
Issue number24
DOIs
StatePublished - Jun 6 2016

Keywords

  • biopolymers
  • elasticity
  • polyproline
  • proteins
  • terahertz spectroscopy

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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