Affiliation:
1. Physics Department, University at Buffalo, USA
Abstract
THz time domain spectroscopy of biomolecules was performed to determine applicability of the technique for chemical and conformational identification of biomolecules. Measurements were performed on samples of DNA, bovine serum albumin, collagen, hen egg white lysozyme, myoglobin, and bacteriorhodopsin as a function of temperature, hydration and photoexcitation. The results are compared to normal mode calculations. We demonstrate a clear resemblance of the observed broad and near featureless THz absorbance spectrum to the calculated density of normal modes. While the magnitude of the absorbance and the center of the broad response depends on biomolecular species, unique chemical identification would appear challenging. The observed dependence on hydration is in agreement with mass and dielectric loading, and the dependence on temperature is in agreement with decreasing conformational flexibility with reduced temperature. Finally THz absorbance dependence on the biomolecular conformation and mutation is demonstrated for bacteriorhodopsin.
Publisher
World Scientific Pub Co Pte Lt
Subject
Electrical and Electronic Engineering,Hardware and Architecture,Electronic, Optical and Magnetic Materials
Cited by
5 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献