Probing Protein Folding with Sequence-Reversed α-Helical Bundles.

ABSTRACT: 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 Spect

SUBMITTER: Kefala A 

PROVIDER: S-EPMC7920257 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature