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

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

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
Volume	2016-November
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

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

Access to Document

10.1109/IRMMW-THz.2016.7758346

Cite this

Ruggiero, MT & Korter, TM 2016, Measuring protein elasticity with terahertz spectroscopy. in 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016. vol. 2016-November, 7758346, 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

@inproceedings{0e0bf80c4bf14102989fa53cd863d4e5,

title = "Measuring protein elasticity with terahertz spectroscopy",

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.",

author = "Ruggiero, {Michael T.} and Korter, {Timothy M.}",

year = "2016",

month = nov,

day = "28",

doi = "10.1109/IRMMW-THz.2016.7758346",

language = "English (US)",

volume = "2016-November",

booktitle = "41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016",

publisher = "IEEE Computer Society",

address = "United States",

note = "41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016 ; Conference date: 25-09-2016 Through 30-09-2016",

}

TY - GEN

T1 - Measuring protein elasticity with terahertz spectroscopy

AU - Ruggiero, Michael T.

AU - Korter, Timothy M.

PY - 2016/11/28

Y1 - 2016/11/28

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=85006152316&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85006152316&partnerID=8YFLogxK

U2 - 10.1109/IRMMW-THz.2016.7758346

DO - 10.1109/IRMMW-THz.2016.7758346

M3 - Conference contribution

AN - SCOPUS:85006152316

VL - 2016-November

BT - 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016

PB - IEEE Computer Society

T2 - 41st International Conference on Infrared, Millimeter and Terahertz Waves, IRMMW-THz 2016

Y2 - 25 September 2016 through 30 September 2016

ER -

Measuring protein elasticity with terahertz spectroscopy

Abstract

Other

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this