Nonlinear infrared spectroscopy of protein conformational change during thermal unfolding
Article Abstract:
Femtosecond two-dimensional infrared spectroscopy such as dispersed vibrational echo spectroscopy and dispersed pump-probe spectroscopy of the amide I vibrations are used to follow the thermal denaturing of ribonuclease A. The findings suggest that nonlinear infrared spectroscopy is an effective probe of proteins conformation that can be used to probe the equilibrium thermodynamics and nonequilibrrium kinetics and dynamics of protein folding.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
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Visualization and characterization of infrared active amide I vibrations of proteins
Article Abstract:
Visualization methods and spatial correlation functions that describe delocalized vibrations of proteins and protein secondary structure are investigated to study the frequency-structure correlations in the amide I vibrational spectroscopy of proteins. Frequency-dependent bright states obtained from doorway mode analysis is characterized to study the vibrational modes revealed in infrared spectroscopy.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
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Residual native structure in a thermally denatured beta-Hairpin
Article Abstract:
The thermal denaturation of trpzip2 between 15 and 82 degree Celsius was studied by using two-dimensional infrared (2D IR) vibrational spectroscopy, dispersed vibrational echo (DVE) spectroscopy, and Fourier transform infrared (FTIR) spectroscopy. Results indicated a significant amount of native structure in the thermally denatured state of trpzip2.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
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