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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Coulomb repulsion in short polypeptides.

Amir Norouzy1, Khaleel I Assaf, Shuai Zhang

  • 1Department of Life Sciences and Chemistry, Jacobs University Bremen , Campus Ring 1, D-28759 Bremen, Germany.

The Journal of Physical Chemistry. B
|December 4, 2014
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Summary
This summary is machine-generated.

Coulomb repulsion in intrinsically disordered polypeptides (IDPs) has minimal impact on anionic chains, contrary to expectations. Cationic chains show unique responses, influenced by side chain characteristics and environmental factors.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Polymer Science

Background:

  • Intrinsically disordered polypeptides (IDPs) are crucial in biological processes.
  • The spatial dimensions and biological activity of IDPs are influenced by electrostatic interactions, particularly Coulomb repulsion between like-charged side chains.
  • Understanding these forces is key to deciphering IDP structure-function relationships.

Purpose of the Study:

  • To investigate the impact of pH-induced charge variations on the structure and dynamics of short, synthetic intrinsically disordered polypeptide models.
  • To challenge the prevailing view of Coulomb repulsion as a dominant force in determining IDP spatial dimensions.
  • To elucidate the interplay of factors governing peptide behavior in response to varying electrostatic conditions.

Main Methods:

  • Utilized two custom time-resolved fluorescence methods: short-distance Förster resonance energy transfer (sdFRET) for end-to-end distances and collision-induced fluorescence quenching (CIFQ) for end-to-end collision rates.
  • Studied acidic (Asp6, Glu6) and basic (Arg6, Lys6, His6) hexapeptides across a pH range of 1 to 12.
  • Incorporated salt screening experiments, N-terminal acetylation, and molecular dynamics simulations for comprehensive analysis.

Main Results:

  • Anionic hexapeptides exhibited no significant dynamical or conformational changes with increasing pH and charge density, even in the presence of salt, contradicting common assumptions.
  • Cationic hexapeptides displayed varied responses to ionization, reflecting the unique properties of each amino acid side chain.
  • Coulomb repulsion between water-solvated side chains is effectively quenched in short peptides unless direct contact occurs.

Conclusions:

  • The influence of Coulomb repulsion on short intrinsically disordered polypeptide conformation and dynamics is less significant than previously thought, especially for anionic chains.
  • Side chain characteristics, local dielectric environment, and solvation play critical roles in modulating peptide behavior.
  • Findings necessitate a refined understanding of electrostatic interactions in short peptide systems and their biological implications.