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Related Concept Videos

Raman Spectroscopy: Overview01:20

Raman Spectroscopy: Overview

The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
However, a small fraction of the scattered light exhibits a frequency shift due to the exchange of energy between the incident photons and the...
Raman Spectroscopy Instrumentation: Overview01:26

Raman Spectroscopy Instrumentation: Overview

A conventional Raman spectrophotometer includes a laser source, a sample holding system, a wavelength selector, and a detector.
The monochromatic laser source, typically using visible or near-infrared radiation, generates a highly focused beam of light. This light interacts with the molecules of the sample, scattering some of the light. Liquid and gaseous samples are usually tested in ordinary glass capillaries, while solids can be analyzed as powders packed in capillaries or as potassium...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
UV–Vis Spectroscopy: Molecular Electronic Transitions01:16

UV–Vis Spectroscopy: Molecular Electronic Transitions

In Ultraviolet–Visible (UV–Vis) spectroscopy, the absorption of electromagnetic radiation is used to probe the electronic structure of molecules. This technique provides insights into molecular electronic transitions, particularly the movement of electrons between different molecular orbitals. Radiation is absorbed if the energy of the electromagnetic radiation passing through the molecule is precisely equal to the energy difference between the excited and ground states. During this process,...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
UV–Vis Spectroscopy of Conjugated Systems01:32

UV–Vis Spectroscopy of Conjugated Systems

Organic compounds with conjugated double bonds show strong absorption features in the UV–visible region of the electromagnetic spectrum attributed to π → π* electronic excitations. Generally, a UV–vis absorption spectrum is recorded as a plot of absorbance vs wavelength. The wavelength of maximum absorbance, which manifests as a peak in the absorption spectrum, is denoted as λmax.
One of the factors influencing λmax is the extent of conjugation in the...

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Related Experiment Video

Updated: Jul 3, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Protein dynamics from time resolved UV Raman spectroscopy.

Gurusamy Balakrishnan1, Colin L Weeks, Mohammed Ibrahim

  • 1Department of Chemistry, University of Washington, Seattle, WA 98195, United States.

Current Opinion in Structural Biology
|July 9, 2008
PubMed
Summary
This summary is machine-generated.

Raman spectroscopy tracks protein structure changes from picoseconds to milliseconds using advanced laser techniques. This method reveals detailed structural information about transient species, aiding in understanding protein unfolding and allostery.

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Last Updated: Jul 3, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Area of Science:

  • Biophysics
  • Spectroscopy
  • Structural Biology

Background:

  • Proteins undergo dynamic structural changes crucial for their function.
  • Understanding these dynamics requires methods capable of probing molecular structure over various timescales.

Purpose of the Study:

  • To review the application of Raman spectroscopy for studying protein structural dynamics.
  • To highlight advancements in pump-probe techniques for accessing picosecond to millisecond timescales.

Main Methods:

  • Utilizing Raman spectroscopy with pump-probe techniques.
  • Tuning probe lasers to resonant electronic transitions (e.g., UV transitions of aromatic residues and peptide bonds).
  • Leveraging advances in laser technology for high-resolution structural characterization.

Main Results:

  • Raman spectroscopy provides unique insights into protein structure evolution.
  • Transient species in protein dynamics can be characterized with unprecedented structural detail.
  • The technique is applicable to studying complex processes like protein unfolding and allostery.

Conclusions:

  • Advanced Raman spectroscopy, particularly pump-probe methods, is a powerful tool for investigating protein dynamics.
  • The ability to probe specific molecular sites offers detailed structural information on transient states.
  • This technique has significant applications in understanding fundamental protein mechanisms.