Far infrared spectra between 4 and 200 cm−1 of poly-l-alanine

Shotts, W.J.; Sievers, A. J.

doi:10.1016/0009-2614(73)80314-8

Cited by 10 publications

(1 citation statement)

References 9 publications

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“…On the experimental side several techniques have been employed by various researchers to study the large-scale motions of biomolecules including small-angle X-ray scattering [3], far-infrared (FIR) absorbance spectra [4, 5, 6, 7, 8] and FIR transmission spectra [9, 10]. Likewise, ultrafast optical-heterodyne-detected Raman-induced Kerr effect spectroscopy (OHD-RIKES) [11] has also been used.…”

Section: Introductionmentioning

confidence: 99%

Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study

Thirumuruganandham

Gómez

Lakshmanan

et al. 2017

IEEE Trans. THz Sci. Technol.

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Infrared (IR) and Terahertz (THz) spectroscopy simulations were carried out using CHARMM35b2 to determine protein stability. The stabilities of three bacterial cold shock proteins (Csps) originating from mesophiles, thermophiles and hyper- thermophiles respectively were investigated in this study. The three different Csps were investigated by Normal-Mode analysis and Molecular Dynamics simulation of THz spectra using the Hessian matrix for solvated systems, interpreted in the harmonic approximation at optimum near-melting temperatures of each homologue, by incorporating differences in the hydrous and anhydrous states of the Csps. The results show slight variations in the large scale protein motion. However, the IR spectra of Csps observed at the low frequency saddle surface region, clearly distinguishes the thermophilic and mesophilic proteins based on their stability. Further studies on protein stability employing low-frequency collective modes have the potential to reveal functionally important conformational changes that are biologically significant.

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Section: Introductionmentioning

confidence: 99%

Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study

Thirumuruganandham

Gómez

Lakshmanan

et al. 2017

IEEE Trans. THz Sci. Technol.

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Low frequency vibrations of amino acid homopolymers observed by synchrotron far-ir absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra

Xie

Miller

et al. 1999

Biopolymers

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The far‐infrared properties of polyamino acids

Shotts

Sievers

1974

Biopolymers

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SynopsisThe far-infrared absorption between 3 and G.30 cm-' of several amino acids and polyamino acids is measured under a variety of conditions. The far-infrared spectra of amino acids and short-chain oliyomerr are extremely temperature dependent with the appearance of numerous narrow absorption lines at 4.2 K. There absorption lines broaden or disappear at 300 K or for absorption measiirenients on samples in solution. For longer polymers, relatively broad nearly temperature-independent absorption lines are observed with little difference between the spedra of polymers in solution or in the solid state. These results are explained in terms of the crystalline order of the samples.

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Far infrared spectra between 4 and 200 cm−1 of poly-l-alanine

Cited by 10 publications

References 9 publications

Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study

Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study

Low frequency vibrations of amino acid homopolymers observed by synchrotron far-ir absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra

The far‐infrared properties of polyamino acids

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