Journal article
Short peptides as predictors for the structure of polyarginine sequences in disordered proteins
Biophysical journal, v 120(4), pp 662-676
16 Feb 2021
PMID: 33453267
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Intrinsically disordered proteins and intrinsically disordered regions are frequently enriched in charged amino acids. Intrinsically disordered regions are regularly involved in important biological processes in which one or more charged residues is the driving force behind a protein-biomolecule interaction. Several lines of experimental and computational evidence suggest that polypeptides and proteins that carry high net charges have a high preference for extended conformations with average end-to-end distances exceeding expectations for self-avoiding random coils. Here, we show that charged arginine residues even in short glycine-capped model peptides (GRRG and GRRRG) significantly affect the conformational propensities of each other when compared with the intrinsic propensities of a mostly unperturbed arginine in the tripeptide GRG. A conformational analysis based on experimentally determined J-coupling constants from heteronuclear NMR spectroscopy and amide I' band profiles from vibrational spectroscopy reveals that nearest-neighbor interactions stabilize extended ,3-strand conformations at the expense of polyproline II and turn conformations. The results from molecular dynamics simulations with a CHARMM36m force field and TI P3P water reproduce our results only to a limited extent. The use of the Ramachandran distribution of the central residue of GRRRG in a calculation of end-to-end distances of polyarginines of different length yielded the expected power law behavior. The scaling coefficient of 0.66 suggests that such peptides would be more extended than predicted by a self-avoiding random walk. Our findings thus support in principle theoretical predictions.
Metrics
Details
- Title
- Short peptides as predictors for the structure of polyarginine sequences in disordered proteins
- Creators
- Bridget Milorey - Drexel UniversityReinhard Schweitzer-Stenner - Drexel UniversityBrian Andrews - Drexel UniversityHarald Schwalbe - Goethe University FrankfurtBrigita Urbanc - Drexel University
- Publication Details
- Biophysical journal, v 120(4), pp 662-676
- Publisher
- Elsevier
- Number of pages
- 15
- Grant note
- MCB-1817650 / National Science Foundation; National Science Foundation (NSF) state of Hesse International Office of Drexel University
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics; Chemistry
- Web of Science ID
- WOS:000630950000008
- Scopus ID
- 2-s2.0-85100379699
- Other Identifier
- 991019167850004721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biophysics