Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Alderson, TR; Lee, JH; Charlier, C; Ying, J; Bax, A.
Propensity for cis-Proline Formation in Unfolded Proteins.
Chembiochem. 2018; 19(1): 37-42.
Doi: 10.1002/cbic.201700548
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- Führende Autor*innen der Med Uni Graz
- Alderson Thomas Reid
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- Abstract:
- In unfolded proteins, peptide bonds involving Pro residues exist in equilibrium between the minor cis and major trans conformations. Folded proteins predominantly contain trans-Pro bonds, and slow cis-trans Pro isomerization in the unfolded state is often found to be a rate-limiting step in protein folding. Moreover, kinases and phosphatases that act upon Ser/Thr-Pro motifs exhibit preferential recognition of either the cis- or trans-Pro conformer. Here, NMR spectra obtained at both atmospheric and high pressures indicate that the population of cis-Pro falls well below previous estimates, an effect attributed to the use of short peptides with charged termini in most prior model studies. For the intrinsically disordered protein α-synuclein, cis-Pro populations at all of its five X-Pro bonds are less than 5 %, with only modest ionic strength dependence and no detectable effect of the previously demonstrated interaction between the N- and C-terminal halves of the protein. Comparison to small peptides with the same amino-acid sequence indicates that peptides, particularly those with unblocked, oppositely charged amino and carboxyl end groups, strongly overestimate the amount of cis-Pro.
- Find related publications in this database (using NLM MeSH Indexing)
- Isomerism - administration & dosage
- Nuclear Magnetic Resonance, Biomolecular - administration & dosage
- Pressure - administration & dosage
- Proline - chemistry
- Protein Denaturation - administration & dosage
- alpha-Synuclein - chemistry, metabolism
- Find related publications in this database (Keywords)
- alpha-synuclein
- cis-proline
- high pressure
- isomerization
- NMR spectroscopy
- protein folding