Probing Protein Folding with Sequence-Reversed α-Helical Bundles.
4-α-helical bundle
RM6 protein
circular dichroism (CD)
coiled-coil proteins
multiangle laser light scattering (MALS)
polypeptide chain directionality
protein folding
rop protein
small angle X-ray scattering (SAXS)
α-helix
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
16 Feb 2021
16 Feb 2021
Historique:
received:
25
01
2021
revised:
11
02
2021
accepted:
11
02
2021
entrez:
6
3
2021
pubmed:
7
3
2021
medline:
27
4
2021
Statut:
epublish
Résumé
Recurrent protein folding motifs include various types of helical bundles formed by α-helices that supercoil around each other. While specific patterns of amino acid residues (heptad repeats) characterize the highly versatile folding motif of four-α-helical bundles, the significance of the polypeptide chain directionality is not sufficiently understood, although it determines sequence patterns, helical dipoles, and other parameters for the folding and oligomerization processes of bundles. To investigate directionality aspects in sequence-structure relationships, we reversed the amino acid sequences of two well-characterized, highly regular four-α-helical bundle proteins and studied the folding, oligomerization, and structural properties of the retro-proteins, using Circular Dichroism Spectroscopy (CD), Size Exclusion Chromatography combined with Multi-Angle Laser Light Scattering (SEC-MALS), and Small Angle X-ray Scattering (SAXS). The comparison of the parent proteins with their retro-counterparts reveals that while the α-helical character of the parents is affected to varying degrees by sequence reversal, the folding states, oligomerization propensities, structural stabilities, and shapes of the new molecules strongly depend on the characteristics of the heptad repeat patterns. The highest similarities between parent and retro-proteins are associated with the presence of uninterrupted heptad patterns in helical bundles sequences.
Identifiants
pubmed: 33669383
pii: ijms22041955
doi: 10.3390/ijms22041955
pmc: PMC7920257
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Peptides
0
RNA-Binding Proteins
0
Rop protein, ColE1 plasmid
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Strategic Reference Framework (NSRF) 2014-2020
ID : ΕΔΒΜ34
Organisme : SOLEIL synchrotron
ID : Proposal ID 20140253
Organisme : SOLEIL synchrotron
ID : Proposal ID 20160538
Organisme : Horizon 2020 Framework Programme
ID : BioStruct-X Proposal ID 7054
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