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Peptide Folding: When Simulation Meets Experiment
Despite the small differences in sequence between the two peptides studied, the simulations correctly predict a left-handed 31-helical fold for the beta-heptapeptide and a right-handed helical Fold for thebeta-hexapeptides.
Bull. Soc. Chim. Fr.
Reversible peptide folding in solution by molecular dynamics simulation.
Long-standing questions on how peptides fold are addressed by the simulation at different temperatures of the reversible folding of a peptide in solution in atomic detail, implying that the search problem in peptide (or even protein) folding is surmountable using dynamics simulations.
The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components.
The origins of the nearly ten-year research program of chemical and biological investigations into peptides based on homologated proteinogenic amino acids are described, and the presence of the additional C--C bonds in the backbones of the new peptides did not give rise to a chaotic increase in their secondary structures as many protein specialists might have expected.
The World of β‐ and γ‐Peptides Comprised of Homologated Proteinogenic Amino Acids and Other Components
Tests with proteolytic enzymes of all types and in vivo examination showed β‐ and γ‐peptides to be completely stable towards proteolysis and, as demonstrated for two β‐ peptides, extraordinarily stable towards metabolism, even when bearing functionalized side chains.
Organic Synthesis—Where now?
This review article is an attempt to sketch the important developments in organic synthesis during the past 25 years, and to project them into the future.—The primary motivations that once induced
'100 years of peptide synthesis': ligation methods for peptide and protein synthesis with applications to beta-peptide assemblies.
A brief survey of the history of peptide chemistry from Theodore Curtius to Emil Fischer to Bruce Merrifield is presented and couplings involving beta2- and beta3-peptides are described (with experimental details).
Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate.
It is demonstrated unambiguously that the completely synthetic complex forms channels that are indistinguishable in their voltage-dependent conductance, in their selectivity for divalent cations, and in their blocking behavior from channels isolated from Escherichia coli.
β-Peptides: a surprise at every turn
A brief account of the results obtained since work started in this area in early 1995 is given, and the prospects for the use of β-peptides as drugs, the construction of large, enzymatically-active β-proteins and their interaction with the natural, α- peptidic counterparts are discussed.
β‐Peptides: Synthesis by Arndt‐Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X‐ray crystallography. Helical secondary structure of
The β-hexapeptide (H-β-HVal-β-HAla-β-HLeu)2-OH (2) was prepared from the component L-β-amino acids by conventional peptide synthesis, including fragment coupling. A cyclo-β-tri- and a