The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution.

@article{Chitnumsub1999TheNO,
  title={The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution.},
  author={Penchit Chitnumsub and Wayne R. Fiori and Hilal A. Lashuel and Humberto Gonz{\'a}lez D{\'i}az and Jeffery W. Kelly},
  journal={Bioorganic \& medicinal chemistry},
  year={1999},
  volume={7 1},
  pages={
          39-59
        }
}
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TLDR
The approach described here takes advantage of template driven hydrophobic clusters and template derived conformational biases to nucleate folding in small peptides, affording β-sheets which subsequently self-associate into fibrils.
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This paper describes the solid-phase syntheses of artificial β-sheets 1−4, which mimic the structure and hydrogen-bonding patterns of protein β-sheets. In these compounds, molecular templates induce
A 2,3‘-Substituted Biphenyl-Based Amino Acid Facilitates the Formation of a Monomeric β-Hairpin-like Structure in Aqueous Solution at Elevated Temperature
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An NMR structural evaluation of heptapeptides incorporating 1 revealed the presence of a hydrophobic cluster involving an aromatic ring of 1 and a side chain of one of the flankingHydrophobic α-amino acids, even though the peptides lack sufficient length to adopt a β-sheet structure.
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Cooperativity is a defining characteristic of protein tertiary structure; partially folded forms are usually less stable than either the native conformation or the denatured state. 1 Cooperativity
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TLDR
A thermodynamic β -sheet propensity scale for all the commonly occurring amino acids in aqueous solution is presented and the relative free energies correlate well with previously derived potential values based on statistical analysis of protein structures.
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A biomolecular Lego set modular method whereby prefabricated building blocks are linked block by block has been developed and applied to the synthesis of peptide-based polymers containing parallel
Context is a major determinant of β-sheet propensity
RESIDUES in β-sheets occur in two distinct tertiary contexts: central strands, bordered on both sides by other β-strands, and edge strands, bordered on only a single side by another β-strand1. The
Cooperative Interaction between the Three Strands of a Designed Antiparallel β-Sheet
We describe the de novo design and characterization of a three stranded antiparallel β-sheet (peptide 1−24) and investigate the interplay between the two sets of weak interactions that occur at the
Mechanism of Stabilization of Helical Conformations of Polypeptides by Water Containing Trifluoroethanol
TLDR
In dilute aqueous solution TFE increases helicity by selectively destabilizing amide functions that are solvent exposed, with the consequence that compact conformations such as helices that maximize intramolecular amide−amide hydrogen bonding and minimize amide solvent exposure are selectively favored.
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