Proton-coupled Spectra

Proton-coupled spectra are nuclear magnetic resonance (NMR) spectra in which interactions between hydrogen nuclei and other magnetically active nuclei remain visible, providing detailed information about molecular structure. These patterns arise from scalar, or J, coupling transmitted through chemical bonds; when proton decoupling is not applied, signals split according to the number and arrangement of coupled hydrogens, and coupling constants reflect the bonding environment. In chemistry, proton-coupled carbon-13 spectra can distinguish carbon atoms bearing different numbers of hydrogens and support assignments in complex molecules. The resulting multiplicities and coupling relationships complement chemical shifts, aiding structure elucidation, reaction monitoring, and studies of molecular connectivity.

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Education

JoVE Core - Chemistry

Emission Spectra

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2020

When solids, liquids, or condensed gases are heated sufficiently, they radiate some of the excess energy as light. Photons produced in this manner have a range of energies, and thereby produce a continuous spectrum in which an unbroken series of wavelengths is present. In contrast to continuous spectra, light can also occur as discrete or line spectra having very narrow linewidths interspersed throughout the spectral regions. Exciting a gas at low partial pressure using an electrical current,...

Proton Exchange Membrane Fuel Cells

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2023

Source: Laboratories of Margaret Workman and Kimberly Frye - Depaul University The United States consumes a large amount of energy – the current rate is around 97.5 quadrillion BTUs annually. The vast majority (90%) of this energy comes from non-renewable fuel sources. This energy is used for electricity (39%), transportation (28%), industry (22%), and residential/commercial use (11%). As the world has a limited supply of these non-renewable sources, the United States (among others) is...

Research

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

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Cited by 21 •

2014

Key steps of protein function, in particular backbone conformational changes and proton transfer reactions, often take place in the microsecond to millisecond time scale. These dynamical processes can be studied by time-resolved step-scan Fourier-transform infrared spectroscopy, in particular for proteins whose function is triggered by light.

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

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Cited by 4 •

2015

The first part of this article shows how to select mutant cell lines expressing vesicular Na+/H+ exchangers at their plasma membrane. The second part provides protocols based on intracellular pH measurements and fast ion uptake, which are used to determine the ion selectivity and the kinetic parameters of these exchangers.

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

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2024

Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others. The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...

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