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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
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Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
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Protein Structure Determination in Living Cells.

Teppei Ikeya1, Peter Güntert2,3,4, Yutaka Ito5

  • 1Department of Chemistry, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0397, Japan. tikeya@tmu.ac.jp.

International Journal of Molecular Sciences
|May 22, 2019
PubMed
Summary

In-cell Nuclear Magnetic Resonance (NMR) spectroscopy is advancing protein structure analysis within living cells. New methods provide direct structural data, overcoming previous limitations for understanding protein behavior in vivo.

Keywords:
non-uniform sampling 2paramagnetic effectsprotein structure determination 1spectrum reconstruction 3structural calculation 4

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • In-cell Nuclear Magnetic Resonance (NMR) spectroscopy studies protein behavior under physiological conditions.
  • Current methods rely on indirect structural information, lacking explicit interatomic distances and angles.
  • Determining direct structural data is crucial for understanding protein functions and properties within cells.

Purpose of the Study:

  • To review progress in protein structure analysis within living systems.
  • To discuss the potential of advanced NMR techniques for in-cell structural determination.
  • To explore future directions for visualizing 3D protein structures in cells.

Main Methods:

  • Utilizing paramagnetic effects for enhanced in-cell structural analysis.
  • Combining limited experimental in-cell NMR data with ab initio protein structure prediction software.
  • Employing Nuclear Overhauser Effect Spectroscopy (NOESY) for detailed conformational analysis.

Main Results:

  • Methodological advances are overcoming challenges like short cell lifetimes and low concentrations.
  • Paramagnetic effects offer significant potential for obtaining direct structural insights.
  • Integrated approaches enable visualization of 3D protein structures in cellular environments.

Conclusions:

  • Direct structural data from in-cell NMR is essential for comprehensive protein understanding.
  • Advanced NMR techniques and computational methods are paving the way for in-cell 3D structure determination.
  • Future research holds promise for detailed structural analysis of proteins in their native cellular context.