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Related Concept Videos

Hydrogen Bonds00:26

Hydrogen Bonds

Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
Hydrogen Bonds Control the World!
Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared.
Hydrogen Bonds01:04

Hydrogen Bonds

A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
Ion Exchange01:17

Ion Exchange

Ion exchange chromatography separates charged molecules from a solution by reversibly exchanging them with mobile, or 'active', ions associated with the oppositely charged stationary phase. This method can be used to separate ions, soften and deionize water, and purify solutions. The polymers comprising the ion-exchange column are high-molecular-weight and chemically stable polymers, crosslinked to be porous and essentially insoluble. They are also functionalized with either acidic or basic...
¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
Gas Exchange and Transport01:20

Gas Exchange and Transport

Gas exchange, the intake of molecular oxygen (O2) from the environment and the outflow of carbon dioxide (CO2) into the environment, is necessary for cellular function. Gas exchange during respiration occurs largely via the movement of gas molecules along pressure gradients. Gas travels from areas of higher partial pressure to areas of lower partial pressure. In mammals, gas exchange occurs in the alveoli of the lungs, which are adjacent to capillaries and share a membrane with them.

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Related Experiment Video

Updated: May 22, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Protein hydrogen exchange: testing current models.

John J Skinner1, Woon K Lim, Sabrina Bédard

  • 1Johnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA. skinnerj@uchicago.edu

Protein Science : a Publication of the Protein Society
|May 1, 2012
PubMed
Summary
This summary is machine-generated.

Protein hydrogen exchange (HX) rates reveal complex determinants beyond surface proximity. Detailed analysis is needed to understand structure-rate relationships for protein dynamics.

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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

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Last Updated: May 22, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes
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A Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) Platform for Investigating Peptide Biosynthetic Enzymes

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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Area of Science:

  • Protein dynamics and structure-function relationships.
  • Biophysical chemistry and nuclear magnetic resonance (NMR) spectroscopy.

Background:

  • Protein hydrogen exchange (HX) is a key process for understanding protein dynamics.
  • Previous hypotheses on HX rate determinants require further investigation.

Purpose of the Study:

  • To investigate the factors influencing protein hydrogen exchange rates.
  • To compare experimental HX rates with existing models for rate determination.

Main Methods:

  • Measurement of HX rates for most backbone amide hydrogens in Staphylococcal nuclease using NMR.
  • Application of a modified analysis to enhance accuracy for faster HX hydrogens.

Main Results:

  • HX rates span over 7 orders of magnitude for both surface and buried hydrogens.
  • Surface proximity does not consistently correlate with fast exchange; buried hydrogens can exchange.
  • Current algorithms struggle to predict exchange rates based solely on local interactions or unfolding.

Conclusions:

  • Existing hypotheses for HX rate determination are insufficient.
  • A detailed, hydrogen-by-hydrogen analysis is crucial for understanding protein structure-rate relationships.
  • Further research is needed to refine models of protein dynamics and HX.