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Related Concept Videos

Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
IR Spectroscopy: Molecular Vibration Overview01:24

IR Spectroscopy: Molecular Vibration Overview

When Infrared (IR) radiation passes through a covalently bonded molecule, the bonds transition from lower to higher vibrational levels. The fundamental vibrational motions that result in infrared absorption can be classified as stretching or bending vibrations.
Stretching vibrations are vibrational motions that occur along the bond line, changing the bond length or distance between two bonded atoms. They are further distinguished as symmetric or asymmetric. In symmetric stretching, the...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
Three-Dimensional Microscopy in Microbiology01:28

Three-Dimensional Microscopy in Microbiology

Three-dimensional imaging techniques are essential in cell biology, allowing researchers to visualize intricate cellular structures with high resolution. Two prominent methods, Differential Interference Contrast Microscopy (DIC) and Confocal Scanning Laser Microscopy (CSLM), provide distinct advantages for imaging live and thick specimens, respectively.Differential Interference Contrast MicroscopyDIC microscopy enhances contrast in transparent, unstained samples by converting phase...
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...

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Updated: May 23, 2026

Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy
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Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy

Published on: December 1, 2023

Three-dimensional structures by two-dimensional vibrational spectroscopy.

Amanda Remorino1, Robin M Hochstrasser

  • 1Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.

Accounts of Chemical Research
|March 31, 2012
PubMed
Summary
This summary is machine-generated.

Two-dimensional infrared (2D IR) spectroscopy enables molecular movies of protein structures in motion. This technique successfully determined the picosecond-level structure of a challenging transmembrane protein, advancing structural biology.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Physical Chemistry
  • Structural Biology
  • Biophysics

Background:

  • Traditional methods like X-ray diffraction and NMR have limitations for capturing time-dependent protein structures, especially for dynamic or transmembrane proteins.
  • Existing techniques struggle to resolve ultrafast equilibrium dynamics or determine structures of rapidly interconverting conformations.
  • There is a critical need for novel experimental approaches to visualize molecular movies of changing chemical structures.

Purpose of the Study:

  • To highlight two-dimensional infrared (2D IR) spectroscopy, specifically 2D vibrational echo, as a powerful method for time-resolved protein structure determination.
  • To demonstrate the application of 2D IR for completely determining the structure of a challenging transmembrane protein within a picosecond time window.
  • To compare multidimensional spectroscopy with established structural biology methods and discuss its potential.

Main Methods:

  • Utilizing two-dimensional infrared (2D IR) spectroscopy, particularly the 2D vibrational echo technique.
  • Employing combined carbon-13-oxygen-18 isotope labels to create vibrational resonance pairs for tracking molecular motion.
  • Analyzing time-domain and frequency-domain experimental and theoretical properties essential for protein structure determination.

Main Results:

  • Successfully determined the complete structure of an integrin family transmembrane protein in a few picoseconds.
  • Demonstrated the capability of 2D IR to overcome limitations of X-ray crystallography and NMR for challenging protein structures.
  • Provided a detailed three-dimensional structure of the αIIb transmembrane homodimer, including precise side chain and backbone atom locations.

Conclusions:

  • Two-dimensional infrared (2D IR) spectroscopy is a viable and powerful approach for time-resolved protein structure determination, offering insights into molecular dynamics.
  • The 2D IR method, enhanced by isotopic labeling, can resolve structures of proteins that are difficult to study with conventional techniques.
  • This study presents a novel 3D structure of a transmembrane homodimer, paving the way for understanding protein function through dynamic structural analysis.