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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...

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Related Experiment Video

Updated: May 17, 2026

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
11:06

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Published on: June 30, 2018

Segmental labeling to study multidomain proteins.

Jing Xue1, David S Burz, Alexander Shekhtman

  • 1Department of Chemistry, State University of New York, Albany, NY 12222, USA.

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

Segmental labeling simplifies complex protein structure studies using Nuclear Magnetic Resonance (NMR). This technique aids in analyzing large proteins and investigating modified protein structures.

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Last Updated: May 17, 2026

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
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Published on: June 30, 2018

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Published on: March 20, 2026

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level
08:29

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for determining protein structures.
  • Studying large multi-domain proteins and post-translationally modified proteins presents significant challenges in NMR structural analysis due to spectral complexity.

Purpose of the Study:

  • To review methodologies and recent applications of segmental labeling for NMR structural studies.
  • To highlight the utility of segmental labeling in reducing spectral complexity and facilitating structural analysis of large and modified proteins.

Main Methods:

  • Segmental labeling involves specifically labeling a segment of a protein with NMR-active nuclei.
  • Detailed protocols for implementing segmental labeling techniques are provided.
  • Application in introducing synthetic fragments for studying post-translational modifications.

Main Results:

  • Segmental labeling significantly reduces NMR spectral complexity.
  • Facilitates structural NMR studies of large multi-domain proteins.
  • Enables the study of post-translationally modified proteins by introducing synthetic fragments.

Conclusions:

  • Segmental labeling is a powerful strategy for advancing NMR structural studies of challenging protein systems.
  • The reviewed methodologies and protocols offer practical guidance for researchers.
  • This technique broadens the scope of proteins amenable to detailed structural investigation using NMR.