Two-dimensional resonance Raman spectroscopy of oxygen- and water-ligated myoglobins

2016 ◽  
Vol 145 (3) ◽  
pp. 034203 ◽  
Author(s):  
Brian P. Molesky ◽  
Zhenkun Guo ◽  
Thomas P. Cheshire ◽  
Andrew M. Moran
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Dimensional Resonance

Elucidation of reactive wavepackets by two-dimensional resonance Raman spectroscopy

2015 ◽  
Vol 143 (12) ◽  
pp. 124202 ◽  
Author(s):  
Zhenkun Guo ◽  
Brian P. Molesky ◽  
Thomas P. Cheshire ◽  
Andrew M. Moran
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Dimensional Resonance

scholarly journals Perspective: Two-dimensional resonance Raman spectroscopy

2016 ◽  
Vol 145 (18) ◽  
pp. 180901 ◽  
Author(s):  
Brian P. Molesky ◽  
Zhenkun Guo ◽  
Thomas P. Cheshire ◽  
Andrew M. Moran
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Dimensional Resonance

scholarly journals Intervalley scattering by acoustic phonons in two-dimensional MoS2 revealed by double-resonance Raman spectroscopy

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Bruno R. Carvalho ◽  
Yuanxi Wang ◽  
Sandro Mignuzzi ◽  
Debdulal Roy ◽  
Mauricio Terrones ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Double Resonance ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Acoustic Phonons ◽  
Intervalley Scattering

Identification of Explosives with Two-Dimensional Ultraviolet Resonance Raman Spectroscopy

2008 ◽  
Vol 62 (8) ◽  
pp. 833-839 ◽  
Author(s):  
Gelu Comanescu ◽  
Charles K. Manka ◽  
Jacob Grun ◽  
Sergei Nikitin ◽  
Daniel Zabetakis
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Ultraviolet Resonance Raman Spectroscopy ◽  
Ultraviolet Resonance Raman

scholarly journals Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding

2013 ◽  
Vol 15 (44) ◽  
pp. 19457 ◽  
Author(s):  
Hao Ren ◽  
Zaizhi Lai ◽  
Jason D. Biggs ◽  
Jin Wang ◽  
Shaul Mukamel
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Peptide Folding ◽  
Two Dimensional ◽  
Spectroscopy Study

scholarly journals Two-dimensional stimulated resonance Raman spectroscopy of molecules with broadband x-ray pulses

2012 ◽  
Vol 136 (17) ◽  
pp. 174117 ◽  
Author(s):  
Jason D. Biggs ◽  
Yu Zhang ◽  
Daniel Healion ◽  
Shaul Mukamel
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
X Ray

scholarly journals Probing Protein Secondary Structure Influence on Active Centers with Hetero Two-Dimensional Correlation (Resonance) Raman Spectroscopy: A Demonstration on Cytochrome C

2021 ◽  
pp. 000370282110289
Author(s):  
Julian Hniopek ◽  
Thomas Bocklitz ◽  
Michael Schmitt ◽  
Jürgen Popp
Keyword(s):  
Raman Spectroscopy ◽  
Structure Function ◽  
Active Center ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Active Centers ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Relationship Of

The functionality of active centers in proteins is governed by the secondary and higher structure of proteins which often lead to structures in the active center that are different from the structures found in protein-free models of the active center. To elucidate this structure–function relationship, it is therefore necessary to investigate both the protein structure and the local structure of the active center. In this work, we investigate the application of hetero (resonance) Raman two-dimensional correlation spectroscopy (2D-COS) to this problem. By employing a combination of near-infrared-Fourier transform-Raman- and vis-resonance Raman spectroscopy, we could show that this combination of techniques is able to directly probe the structure–function relationship of proteins. We were able to correlate the transition of the heme center in cytochrome c from low to high spin with changes in the secondary structure with the above mentioned two spectroscopic in situ techniques and without sample preparation. Thereby, we were able to reveal that the combination of a spectroscopic method to selectively observe the active center with a technique that monitors the whole system offers a promising toolkit to investigate the structure–function relationship of proteins with photoactive centers in general.

Nanosecond Two-Dimensional Resonance Raman Correlation Spectroscopy of Benzil Radical Anion

1993 ◽  
Vol 47 (9) ◽  
pp. 1343-1344 ◽  
Author(s):  
Ken Ebihara ◽  
Hiroaki Takahashi ◽  
Isao Noda
Keyword(s):  
Raman Spectra ◽  
Radical Anion ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Correlation Method ◽  
External Perturbation ◽  
Correlation Spectroscopy ◽  
Two Dimensional ◽  
Time Resolved ◽  
Dimensional Resonance

Nanosecond two-dimensional resonance Raman spectroscopy was used to investigate the photochemistry of the production and decay of the radical anion of benzil in various solvents. A newly developed correlation formalism was applied to a set of time-resolved resonance Raman spectra of the benzil radical anion to generate two-dimensional Raman spectra. Unlike the 2D correlation method previously developed for IR spectroscopy, which was based on signals induced by a sinusoidally varying external perturbation, the new correlation formalism is generally applicable to the studies of any transient spectroscopic signals having an arbitrary waveform. This makes it ideally suited for the analysis of time-resolved spectroscopic signals following photoexcitation. 2D Raman spectra effectively accentuate certain useful information which is sometimes obscured in the original time-resolved spectra. Spectral intensity changes and peak shifts arising from the photochemical reaction processes were clearly observed by the synchronous and asynchronous correlation.

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