Proteomimetics as protein-inspired scaffolds with defined tertiary ...
WEBFeb 6, 2020 — The ability to mimic isolated helical secondary structures with heterogeneous backbones has been leveraged to produce mimics of a bioactive helix–turn–helix tertiary scaffold in which the...
How physical forces drive the process of helical membrane protein folding
WEBFeb 8, 2022 — In essence, membrane protein folding is determined by the interactions between the protein residues themselves and their surrounding environment. Any discussion of folding must thus begin with helix residue …
α-Helical Protein Assembly Motifs - Journal of Biological Chemistry
WEBThis review will focus on α-helical protein assembly motifs where the α-helix is the major element of secondary structure involved in the folding and stability of the structure and may also be involved in function by binding to receptor molecules.
Tertiary Protein Structure and Folds | SWISS-MODEL - Expasy
WEBThe globin fold usually consists of eight alpha-helices. The two helices at the end of the chain are antiparallel, forming alpha helix-turn-helix motif, but the remainder of the fold does not include any characterised super-secondary structures.
Energy landscape underlying spontaneous insertion and folding …
WEBNov 23, 2018 — A recent force spectroscopy study of the folding of an α -helical membrane protein, GlpG, showed that the folded state has a very high kinetic stability and a relatively low thermodynamic...
Fundamental processes of protein folding: Measuring the …
WEBJan 1, 2009 — The pathway of protein folding, the rate of folding, and the final folded structure should be predictable if the energetic contributions to folding of these fundamental factors were properly understood. αtα is a helix-turn-helix peptide that was developed by de novo design to provide a model system for the study of these important elements of ...
WEBFeb 8, 2022 — protein folding biophysics. Despite the greater challenge, better model systems and new experimental techniques are starting to unravel the forces and pathways in membrane protein folding. Keywords co-translational folding; energetics; folding pathways; helix inser-tion; membrane protein topology
Folding Mechanism of a Helix-Turn-Helix Protein from …
WEBFeb 2, 2011 — Helix-turn-helix motifs are important super-secondary protein structural elements and excellent models for studying the mechanism of protein folding. We have been investigating folding of a de novo designed 38-residue helix-turn-helix motif alpha-t-alpha using IR spectroscopy with site-specific 13C isotopic editing.
Rationally designed helix-turn-helix proteins and their …
WEBJul 1, 1995 — Circular dichroism and electrophoretic mobility shift studies were performed to confirm that dimerized N-terminal domains of bacterial repressors containing helix-turn-helix motifs are capable of high-affinity and specific DNA recognition as opposed to the monomeric N-terminal domains.
The complete folding pathway of a protein from nanoseconds to ...
WEBFeb 20, 2003 — Ultrafast-folding proteins fold and unfold on timescales accessible by both approaches 4, 5, so here we study the folding pathway of the three-helix bundle protein Engrailed...
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