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Molecular dynamics simulations of signal transmission through a glycine peptide chain
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View: Figures


Image of FIG. 1.
FIG. 1.

(Color online) Schematic drawing of methanethiolate capped glycine binding with the Au clusters. Section in brackets shows two residue. GLY1000 is composed by 1000 glycine residues with a total length of about . GLY1000 is chemically a very soft molecule due to the lack of side groups on the carbon (the one in between the CO group and the N atom). The black dotted line arrow indicates the vibration direction of the C–N bond where the signal is applied.

Image of FIG. 2.
FIG. 2.

(a) Carrier signal, (b) information or base band signal, and (c) carrier signal modulated by the amplitude of the base band signal.

Image of FIG. 3.
FIG. 3.

(Color online) Frequency (left) and time domain representations of the recovered signal (center) and its rectified and low pass filtered signal (right) from the first [(a)–(c)], second [(d)–(f)], sixth [(g)–(i)], and eleventh [(j)–(l)] CN bonds along the molecular chain. Band pass filter central frequency is with a bandwidth of . Low pass filter cutoff frequency is .

Image of FIG. 4.
FIG. 4.

(Color online) Base band signals recovered at the 499th, 495th, 490th, and 485th [panels (a)–(d), respectively] as well as at the 501st, 505th, 510th, and 515th [panels (e)–(h), respectively] CN bonds when the signal is inserted at the 500th CN bond. A low pass filter with a cutoff frequency of is use for all the signals.

Image of FIG. 5.
FIG. 5.

(Color online) Spectra (left), modulated signal (center), and recovered base band signal (right) at the 501st [(a)–(c)], 505th [(d)–(f)], 510th [(g)–(i)], and 515th [(j)–(l)] CN bonds along the molecular chain after performing molecular dynamics simulations at temperature of .


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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Molecular dynamics simulations of signal transmission through a glycine peptide chain