Journal article
Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor Interactions between Unlike Residues
Chemistry : a European journal, v 21(13), pp 5173-5192
23 Mar 2015
PMID: 25728043
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
To explore the influence of nearest neighbors on conformational biases in unfolded peptides, we combined vibrational and 2D NMR spectroscopy to obtain the conformational distributions of selected "GxyG" host-guest peptides in aqueous solution: GDyG, GSyG, GxLG, GxVG, where x/y= A, K, L, V. Large changes of conformational propensities were observed due to nearest-neighbor interactions, at variance with the isolated pair hypothesis. We found that protonated aspartic acid and serine lose their above-the-average preference for turn-like structures in favor of polyproline II (pPII) populations in the presence of neighbors with bulky side chains. Such residues also decrease the above-the-average pPII preference of alanine. These observations suggest that the underlying mechanism involves a disruption of the hydration shell. Thermodynamic analysis of (3)J(H-N, H-alpha) (T) data for each x, y residue reveals that modest changes in the conformational ensemble masks larger changes of enthalpy and entropy governing the pPII <->beta equilibrium indicating a significant residue dependent temperature dependence of the peptides' conformational ensembles. These results suggest that nearest-neighbor interactions between unlike residues act as conformational randomizers close to the enthalpy-entropy compensation temperature, eliminating intrinsic biases in favor of largely balanced pPII/beta dominated ensembles at physiological temperatures.
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Details
- Title
- Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor Interactions between Unlike Residues
- Creators
- Siobhan E. Toal - Drexel UniversityNina Kubatova - Goethe University FrankfurtChristian Richter - Goethe University FrankfurtVerena Linhard - Goethe University FrankfurtHarald Schwalbe - Goethe University FrankfurtReinhard Schweitzer-Stenner - Drexel University
- Publication Details
- Chemistry : a European journal, v 21(13), pp 5173-5192
- Publisher
- Wiley
- Number of pages
- 20
- Grant note
- College of Arts and Sciences State of Hessen (Center for Biomolecular Magnetic Resonance) DFG; German Research Foundation (DFG); European Commission
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]; Chemistry
- Web of Science ID
- WOS:000352140000036
- Scopus ID
- 2-s2.0-84924703700
- Other Identifier
- 991019167626904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Chemistry, Multidisciplinary