What is it about?
Peptide and protein design involves experimentally characterizing the building blocks using chemical constructs. I have been successful in experimentally establishing the design of beta-hairpin motifs using synthetic peptides. This study is the first study to investigate the folding of hydrophobic linear peptide sequences into beta hairpins using computational methods.
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Why is it important?
This is an important step in investigating the folding of synthetic peptides harboring non-natural amino acids as nucleating agents of protein folds (beta-turns). This study clearly establishes that we can computationally investigate the folding of short peptide segments, before investing in them experimentally.
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This page is a summary of: Ultrafast folding and molecular dynamics of a linear hydrophobic β-hairpin, Journal of Biomolecular Structure and Dynamics, December 2013, Taylor & Francis,
DOI: 10.1080/07391102.2012.738612.
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