Background: Intrinsically disordered proteins and protein regions
(IDPs/IDRs) are important in diverse biological processes. Lacking a stable
secondary structure, they display an ensemble of conformations. One factor
contributing to this conformational heterogeneity is the proline
cis/trans isomerization. The knowledge and value of a given
cis/trans proline ratio are paramount, as the different conformational
states can be responsible for different biological functions. Nuclear Magnetic
Resonance (NMR) spectroscopy is the only method to characterize the two
co-existing isomers on an atomic level, and only a few works report on these
data. Methods: After collecting the available experimental literature
findings, we conducted a statistical analysis regarding the influence of the
neighboring amino acid types (i
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Original Research
Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides
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1
Analytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, 1117 Budapest, Hungary
2
Department of Medical Chemistry, University of Szeged, 6720 Szeged, Hungary
3
Hevesy György PhD School of Chemistry, Eötvös Loránd University, 1117 Budapest, Hungary
*Correspondence: andrea.bodor@ttk.elte.hu (Andrea Bodor)
Front. Biosci. (Landmark Ed) 2023, 28(6), 127;
https://doi.org/10.31083/j.fbl2806127
Submitted: 17 April 2023 | Revised: 15 May 2023 | Accepted: 26 May 2023 | Published: 29 June 2023
(This article belongs to the Special Issue Protein Folding, Misfolding, Non-Folding, and Assembly)
Copyright: © 2023 The Author(s). Published by IMR Press.
This is an open access article under the CC BY 4.0 license.
Abstract
Keywords
intrinsically disordered proteins
NMR spectroscopy
proline
cis/trans isomerization
statistical analysis
Funding
NKFI K124900/National Research, Development and Innovation Office
K137940/National Research, Development and Innovation Office
TKP2020-NKA-06/the ELTE Thematic Excellence Programme 2020, National Challenges Subprogramme
Figures
Fig. 1.