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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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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.
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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How sequence determines elasticity of disordered proteins.

Shanmei Cheng1, Murat Cetinkaya, Frauke Gräter

  • 1German Max Planck Society-Chinese Academy of Sciences Partner Institute and Key Laboratory for Computational Biology, Shanghai Institute for Biological Sciences, Shanghai, China.

Biophysical Journal
|December 16, 2010
PubMed
Summary

Nature designs disordered proteins for elasticity by tuning sequences. Molecular dynamics simulations reveal that while proline and glycine content are indicators, polyproline II content and nonlocal forces like electrostatics significantly influence coiling properties and protein elasticity.

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Area of Science:

  • Biophysics
  • Protein Science
  • Materials Science

Background:

  • Disordered proteins exhibit unique elastomeric properties crucial for biological functions.
  • Understanding the sequence-elasticity relationship in these proteins is key to harnessing their capabilities.

Purpose of the Study:

  • To investigate how natural disordered proteins achieve specific coiling properties and elasticity.
  • To elucidate the relationship between protein sequence and mechanical properties.

Main Methods:

  • Extensive explicit solvent molecular dynamics simulations were performed on four natural elastomeric disordered proteins: FG repeats, resilin, PPAK, and spider silk.
  • Force-extension curves were generated and compared to models of purely entropic coiling.

Main Results:

  • While proline and glycine content generally indicate entropic elasticity, deviations from simple additivity were observed.
  • Coiling propensities correlated more strongly with polyproline II content than proline content.
  • Nonlocal interactions, such as electrostatic forces, significantly enhanced coiling, especially in glycine-rich regions, leading to distinct features like resilin's force-extension curve hump.

Conclusions:

  • Protein sequence, particularly polyproline II content and nonlocal interactions, plays a critical role in tuning the elasticity of disordered proteins.
  • Evolution has optimized these sequences for diverse elastomeric functions.
  • Findings provide testable hypotheses for experimental validation using force spectroscopy.