Journal ArticleDOI
Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding.
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TLDR
It is shown that β-lactoglobulin, which consists predominantly of β-sheets, exhibited a markedly high propensity to form an α–-helical structure in the presence of TFE, as measured by far-UV circular dichroism.About:
This article is published in Journal of Molecular Biology.The article was published on 1995-01-13. It has received 429 citations till now. The article focuses on the topics: Protein secondary structure & Protein folding.read more
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Principles of protein folding--a perspective from simple exact models.
Ken A. Dill,Sarina Bromberg,Kaizhi Yue,Klaus M. Fiebig,David P. Yee,Paul Thomas,Hue Sun Chan +6 more
TL;DR: These studies suggest the possibility of creating “foldable” chain molecules other than proteins, and can account for the properties that characterize protein folding: two‐state cooperativity, secondary and tertiary structures, and multistage folding kinetics.
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Designing conditions for in vitro formation of amyloid protofilaments and fibrils
Fabrizio Chiti,Paul Webster,Niccolò Taddei,Anne Clark,Massimo Stefani,Giampietro Ramponi,Christopher M. Dobson +6 more
TL;DR: The results indicate that formation of amyloid occurs when the native fold of a protein is destabilized under conditions in which noncovalent interactions, and in particular hydrogen bonding, within the polypeptide chain remain favorable.
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Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
Margitta Dathe,Torsten Wieprecht +1 more
TL;DR: This review is concerned with the influence of structural parameters, such as peptide helicity, hydrophobicity,hydrophobic moment, peptide charge and the size of the hydrophobic/hydrophilic domain, on membrane activity and selectivity of natural and model peptides.
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Protein folding in the landscape perspective: Chevron plots and non‐arrhenius kinetics
Hue Sun Chan,Ken A. Dill +1 more
TL;DR: Two simple models and the energy landscape perspective are used to study protein folding kinetics and it is found that unfolding is not always a direct reversal of the folding process.
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Polymer principles and protein folding.
TL;DR: The emerging role of statistical mechanics and polymer theory in protein folding is surveyed, finding that in the polymer perspective, the folding code is more a solvation code than a code of local ØΨ propensities.