4.8 Article

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

期刊

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 24, 页码 6877-6881

出版社

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201602268

关键词

biopolymers; elasticity; polyproline; proteins; terahertz spectroscopy

资金

  1. National Science Foundation [CHE-1301068]
  2. Royal Society International Exchanges Scheme
  3. Royal Society of Chemistry JWT Jones Travelling Fellowship
  4. U.K. Engineering and Physical Sciences Research Council [EP/J007803/1]
  5. EPSRC [EP/J007803/1] Funding Source: UKRI
  6. Engineering and Physical Sciences Research Council [EP/J007803/1] Funding Source: researchfish

向作者/读者索取更多资源

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.

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