Structure and elasticity mechanism of full length resilin proteins

Xiao Hu; Guokui Qin; Peggy Cebe; David L. Kaplan

doi:10.1109/NEBC.2010.5458182

Structure and elasticity mechanism of full length resilin proteins

Xiao Hu, Guokui Qin, Peggy Cebe, David L. Kaplan

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

Abstract

Full length resilin, as well as resilin peptides encoded by exons 1 and 3, were analyzed for structural features. The elasticity mechanisms of resilin related to insect function are described. To approach this goal, a simple energy input method based on thermal treatment was used to detail the transitions and structures of resilin. A systematic pathway to the mechanism was followed based on Temperature-modulated Differential Scanning Calorimetry (TMDSC), Real-time Fourier Transform Infrared Spectroscopy (FTIR), synchrotron Real-time X-ray, and AFM. The results revealed that the conformation and transition of resilin proteins played a critical role for their elastic mechanisms, which provided an effective pathway to design new super elastic biomaterials.

Original language	English (US)
Title of host publication	Proceedings of the 2010 IEEE 36th Annual Northeast Bioengineering Conference, NEBEC 2010
DOIs	https://doi.org/10.1109/NEBC.2010.5458182
State	Published - Jun 8 2010
Externally published	Yes
Event	36th Annual Northeast Bioengineering Conference, NEBEC 2010 - New York, NY, United States Duration: Mar 26 2010 → Mar 28 2010

Other

Other	36th Annual Northeast Bioengineering Conference, NEBEC 2010
Country/Territory	United States
City	New York, NY
Period	3/26/10 → 3/28/10

All Science Journal Classification (ASJC) codes

Bioengineering

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10.1109/NEBC.2010.5458182

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title = "Structure and elasticity mechanism of full length resilin proteins",

abstract = "Full length resilin, as well as resilin peptides encoded by exons 1 and 3, were analyzed for structural features. The elasticity mechanisms of resilin related to insect function are described. To approach this goal, a simple energy input method based on thermal treatment was used to detail the transitions and structures of resilin. A systematic pathway to the mechanism was followed based on Temperature-modulated Differential Scanning Calorimetry (TMDSC), Real-time Fourier Transform Infrared Spectroscopy (FTIR), synchrotron Real-time X-ray, and AFM. The results revealed that the conformation and transition of resilin proteins played a critical role for their elastic mechanisms, which provided an effective pathway to design new super elastic biomaterials.",

author = "Xiao Hu and Guokui Qin and Peggy Cebe and Kaplan, {David L.}",

year = "2010",

month = jun,

day = "8",

doi = "10.1109/NEBC.2010.5458182",

language = "English (US)",

isbn = "9781424468799",

booktitle = "Proceedings of the 2010 IEEE 36th Annual Northeast Bioengineering Conference, NEBEC 2010",

note = "36th Annual Northeast Bioengineering Conference, NEBEC 2010 ; Conference date: 26-03-2010 Through 28-03-2010",

}

TY - GEN

T1 - Structure and elasticity mechanism of full length resilin proteins

AU - Hu, Xiao

AU - Qin, Guokui

AU - Cebe, Peggy

AU - Kaplan, David L.

PY - 2010/6/8

Y1 - 2010/6/8

N2 - Full length resilin, as well as resilin peptides encoded by exons 1 and 3, were analyzed for structural features. The elasticity mechanisms of resilin related to insect function are described. To approach this goal, a simple energy input method based on thermal treatment was used to detail the transitions and structures of resilin. A systematic pathway to the mechanism was followed based on Temperature-modulated Differential Scanning Calorimetry (TMDSC), Real-time Fourier Transform Infrared Spectroscopy (FTIR), synchrotron Real-time X-ray, and AFM. The results revealed that the conformation and transition of resilin proteins played a critical role for their elastic mechanisms, which provided an effective pathway to design new super elastic biomaterials.

AB - Full length resilin, as well as resilin peptides encoded by exons 1 and 3, were analyzed for structural features. The elasticity mechanisms of resilin related to insect function are described. To approach this goal, a simple energy input method based on thermal treatment was used to detail the transitions and structures of resilin. A systematic pathway to the mechanism was followed based on Temperature-modulated Differential Scanning Calorimetry (TMDSC), Real-time Fourier Transform Infrared Spectroscopy (FTIR), synchrotron Real-time X-ray, and AFM. The results revealed that the conformation and transition of resilin proteins played a critical role for their elastic mechanisms, which provided an effective pathway to design new super elastic biomaterials.

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U2 - 10.1109/NEBC.2010.5458182

DO - 10.1109/NEBC.2010.5458182

M3 - Conference contribution

AN - SCOPUS:77953035955

SN - 9781424468799

BT - Proceedings of the 2010 IEEE 36th Annual Northeast Bioengineering Conference, NEBEC 2010

T2 - 36th Annual Northeast Bioengineering Conference, NEBEC 2010

Y2 - 26 March 2010 through 28 March 2010

ER -

Structure and elasticity mechanism of full length resilin proteins

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