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.
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 ...
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...
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.
WEBFeb 8, 2022 · Subsequent helix insertion is influenced by the orientation of, and interactions with, previously inserted helices, as well as interactions with other proteins in the translocon complex. As helices emerge from the translocon, folding can begin and helical hairpin folding units may be preferred.
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.
Folding Pathways of a Helix−Turn−Helix Model Protein
WEBAug 21, 1997 · Their folding pathways show a fast initial development of a helix−bend−helix motif, followed by a dynamic behavior predicted by the diffusion−collision model of Karplus and Weaver. The phenomenology of the pathways is consistent with experimental results.
Protein Motifs: the Helix-Turn-Helix Motif - Wiley Online Library
WEBSep 28, 2007 · Abstract. The helix-turn-helix motif was first observed in the structures of certain proteins that bind to specific regulatory sites on deoxyribonucleic acid (DNA). It is made up of a part of the protein comprising an α-helix followed by a turn followed by a second α-helix aligned approximately 120° to the first.
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