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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...
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range. Consider...
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei in a...
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...

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Raman spectroscopy of proteins and nucleoproteins.

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A structural model for the single-stranded DNA genome of filamentous bacteriophage Pf1.

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Raman tensors and their application in structural studies of biological systems.

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Related Experiment Video

Updated: Jul 5, 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

Raman spectroscopy of proteins.

James M Benevides1, Stacy A Overman1, George J Thomas1

  • 1University of Missouri-Kansas City, School of Biological Sciences, Kansas City, Missouri.

Current Protocols in Protein Science
|April 23, 2008
PubMed
Summary

Raman spectroscopy reveals protein structure and dynamics by analyzing vibrational modes. This technique provides insights into protein folding, assembly, and interactions, serving as a powerful tool for structural biology.

Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Protein Raman spectra exhibit bands sensitive to secondary, tertiary, and quaternary structures.
  • Spectral features reflect side-chain orientations and local environments, acting as signatures for protein 3D structure.
  • Raman spectroscopy can probe intramolecular dynamics and intermolecular interactions.

Purpose of the Study:

  • To illustrate the strengths of Raman spectroscopy in structural biology.
  • To showcase applications in understanding protein folding, assembly, and interactions.
  • To survey conventional, UV-resonance, and polarized Raman techniques.

Main Methods:

  • Analysis of protein Raman spectra, including band positions, intensities, and polarizations.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Related Experiment Videos

Last Updated: Jul 5, 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

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

  • Application of Raman spectroscopy to study bacteriophage P22 capsid assembly.
  • Investigation of subunit orientations in filamentous viruses using Raman spectroscopy.
  • Examination of cysteine hydrogen bonding in viral protein folding and function.
  • Study of structural determinants in protein/DNA recognition in gene regulatory complexes.

    • Main Results:

    • Raman spectroscopy provides empirical signatures of protein three-dimensional structure.
    • The technique elucidates subunit folding, recognition, and assembly processes.
    • Side-chain and main-chain orientations in viral proteins are determined.
    • Cysteine hydrogen bonding roles in protein folding and function are revealed.
    • Structural factors governing protein/DNA recognition are identified.

    Conclusions:

    • Raman spectroscopy is a versatile tool for characterizing protein structure, dynamics, and interactions.
    • Applications demonstrate its utility in studying complex biological systems like viruses and gene regulatory complexes.
    • Different Raman techniques offer complementary information for comprehensive structural analysis.