Measuring protein elasticity with terahertz spectroscopy

Michael T. Ruggiero; Timothy M. Korter

doi:10.1109/IRMMW-THz.2016.7758346

Measuring protein elasticity with terahertz spectroscopy

Michael T. Ruggiero, Timothy M. Korter

Research output: Chapter in Book/Entry/Poem › Conference contribution

1 Scopus citations

Abstract

Elasticity is a key parameter in evaluating the structural stability of large polymeric molecules such as polysaccharides and polypeptides. The determination of the elastic parameters of complex biomolecules has been a long-standing challenge and terahertz spectroscopy is emerging as an ideal approach for such measurements. A new methodology is presented here, combining time-domain terahertz spectroscopy, X-ray diffraction, and solid-state density functional theory to achieve high-accuracy values for the Young's moduli of biopolymers. The capabilities are demonstrated by application of this method to crystalline poly-L-proline helices and other polypeptides.

Original language	English (US)
Title of host publication	41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016
Publisher	IEEE Computer Society
ISBN (Electronic)	9781467384858
DOIs	https://doi.org/10.1109/IRMMW-THz.2016.7758346
State	Published - Nov 28 2016
Event	41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016 - Copenhagen, Denmark Duration: Sep 25 2016 → Sep 30 2016

Publication series

Name	International Conference on Infrared, Millimeter, and Terahertz Waves, IRMMW-THz
Volume	2016-November
ISSN (Print)	2162-2027
ISSN (Electronic)	2162-2035

Other

Other	41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016
Country/Territory	Denmark
City	Copenhagen
Period	9/25/16 → 9/30/16

ASJC Scopus subject areas

Energy Engineering and Power Technology
Electrical and Electronic Engineering

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10.1109/IRMMW-THz.2016.7758346

Cite this

Ruggiero, M. T., & Korter, T. M. (2016). Measuring protein elasticity with terahertz spectroscopy. In 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016 Article 7758346 (International Conference on Infrared, Millimeter, and Terahertz Waves, IRMMW-THz; Vol. 2016-November). IEEE Computer Society. https://doi.org/10.1109/IRMMW-THz.2016.7758346

Measuring protein elasticity with terahertz spectroscopy. / Ruggiero, Michael T.; Korter, Timothy M.
41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016. IEEE Computer Society, 2016. 7758346 (International Conference on Infrared, Millimeter, and Terahertz Waves, IRMMW-THz; Vol. 2016-November).

Research output: Chapter in Book/Entry/Poem › Conference contribution

Ruggiero, MT & Korter, TM 2016, Measuring protein elasticity with terahertz spectroscopy. in 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016., 7758346, International Conference on Infrared, Millimeter, and Terahertz Waves, IRMMW-THz, vol. 2016-November, IEEE Computer Society, 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016, Copenhagen, Denmark, 9/25/16. https://doi.org/10.1109/IRMMW-THz.2016.7758346

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abstract = "Elasticity is a key parameter in evaluating the structural stability of large polymeric molecules such as polysaccharides and polypeptides. The determination of the elastic parameters of complex biomolecules has been a long-standing challenge and terahertz spectroscopy is emerging as an ideal approach for such measurements. A new methodology is presented here, combining time-domain terahertz spectroscopy, X-ray diffraction, and solid-state density functional theory to achieve high-accuracy values for the Young's moduli of biopolymers. The capabilities are demonstrated by application of this method to crystalline poly-L-proline helices and other polypeptides.",

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AB - Elasticity is a key parameter in evaluating the structural stability of large polymeric molecules such as polysaccharides and polypeptides. The determination of the elastic parameters of complex biomolecules has been a long-standing challenge and terahertz spectroscopy is emerging as an ideal approach for such measurements. A new methodology is presented here, combining time-domain terahertz spectroscopy, X-ray diffraction, and solid-state density functional theory to achieve high-accuracy values for the Young's moduli of biopolymers. The capabilities are demonstrated by application of this method to crystalline poly-L-proline helices and other polypeptides.

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Measuring protein elasticity with terahertz spectroscopy

Abstract

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