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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Stereoisomers02:32

Stereoisomers

On the basis of mirror symmetry, stereoisomers of an organic molecule can be further classified into diastereomers and enantiomers. Diastereomers are stereoisomers that are not mirror images of each other. Substituted alkenes, such as the cis and trans isomers of 2-butene, are diastereomers, as these molecules exhibit different spatial orientations of their constituent atoms, are not mirror images of each other, and do not interconvert. Here, the interconversion is suppressed due to restricted...
Stereoisomerism02:52

Stereoisomerism

Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula.
Transition metal complexes often exist as geometric isomers, in which the same atoms are connected through the same types of bonds but with differences in their orientation in space. Coordination complexes with two different ligands in the cis and trans positions from a ligand of interest form isomers. For example, the octahedral [Co(NH3)4Cl2]+ ion has two isomers (Figure 1) In the cis...
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...

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Related Experiment Video

Updated: May 17, 2026

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

Stereo-array isotope labeling method for studying protein structure and dynamics.

Yohei Miyanoiri1, Mitsuhiro Takeda, Masatsune Kainosho

  • 1Graduate School of Science, Nagoya University, Nagoya, Japan.

Advances in Experimental Medicine and Biology
|October 19, 2012
PubMed
Summary
This summary is machine-generated.

The stereo-array isotope labeling (SAIL) method uses optimized isotope labeling patterns for NMR studies. This technique facilitates high-resolution structure determination and protein dynamics investigations.

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Last Updated: May 17, 2026

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

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Published on: April 17, 2017

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Published on: August 23, 2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for studying protein structure and dynamics.
  • Isotope labeling is a key technique to enhance NMR signal resolution and interpretation.
  • Challenges exist in labeling large or complex proteins for detailed NMR analysis.

Purpose of the Study:

  • To introduce the applications of the stereo-array isotope labeling (SAIL) method.
  • To highlight how SAIL facilitates advanced NMR studies.
  • To showcase the utility of SAIL in structural biology and protein dynamics.

Main Methods:

  • The stereo-array isotope labeling (SAIL) method involves incorporating chemically synthesized amino acids with specific isotope labeling patterns.
  • SAIL can be implemented using either cell-free protein synthesis systems or cellular expression systems.
  • Labeling patterns are optimized for specific Nuclear Magnetic Resonance (NMR) experiments.

Main Results:

  • The SAIL method has been instrumental in enabling a wide range of novel investigations over the past decade.
  • It facilitates high-resolution structure determinations of large proteins.
  • SAIL aids in the detailed investigation of protein dynamics.

Conclusions:

  • The SAIL method is a powerful approach for advanced NMR studies of proteins.
  • It significantly contributes to understanding protein structure and dynamics.
  • SAIL-related strategies offer versatile applications in structural biology research.