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Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 08/2018, Volume 140, Issue 30, pp. 9396 - 9399
A thiol-thioester exchange system has been used to measure the propensities of diverse β-amino acid residues to participate in an α-helix-like conformation.... 
FORMING TENDENCIES | DESIGN | PEPTIDES | PROTEIN | RECOGNITION | SIDE-CHAIN | BIOSYNTHESIS | STABILITY | FOLDAMERS | CHEMISTRY, MULTIDISCIPLINARY | Amino Acid Sequence | Protein Conformation, alpha-Helical | Thermodynamics | Peptides - chemical synthesis | Peptides - chemistry | Amino Acids - chemistry | Molecular Structure | Amino Acids - chemical synthesis
Journal Article
Current opinion in structural biology, ISSN 0959-440X, 2016, Volume 39, pp. 96 - 105
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 09/2017, Volume 139, Issue 38, pp. 13292 - 13295
We describe the use of thioester exchange equilibria to measure the propensities of amino acid residues to participate in helical secondary structure at room... 
ALPHA-HELIX | PEPTIDES | PROTEIN | MODIFIED RIBOSOMES | BETA-SHEET | STABILITY | FOLDAMERS | SECONDARY STRUCTURE | PARAMETERS | COILED-COIL | CHEMISTRY, MULTIDISCIPLINARY
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 10/2018, Volume 140, Issue 39, pp. 12476 - 12483
What is the best spatial arrangement of a pair of reactive groups for bifunctional catalysis of a chemical transformation? The conformational versatility of... 
ALPHA/BETA-PEPTIDES | DESIGN | PEPTIDE-BASED CATALYSTS | STEREOSELECTIVITY | ENZYMES | CONDENSATION | IMIDAZOLE | BETA-PEPTIDES | SELECTIVITY | CHEMISTRY, MULTIDISCIPLINARY | OLIGOMERS
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 08/2016, Volume 138, Issue 34, pp. 10766 - 10769
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2010, Volume 132, Issue 23, pp. 7868 - 7869
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO···HN H-bonds), a secondary structure that is formed by oligomers... 
TURNS | DESIGN | MIMICRY | RECOGNITION | NANOCAVITIES | CHEMISTRY, MULTIDISCIPLINARY | HYBRID PEPTIDES | CONFORMATIONS | Peptides - metabolism | Hydrogen Bonding | Peptides - chemistry | Protein Structure, Secondary | Solutions | Amino Acids - analysis | Amino Acids - chemistry | Models, Molecular | Crystallography, X-Ray | Protein Folding
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 10/2010, Volume 132, Issue 39, pp. 13879 - 13885
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 01/2018, Volume 140, Issue 4, pp. 1394 - 1400
We have evaluated the impact of changes in the chemical structure of peptidic oligomers containing α-, β-, and γ-amino acid residues (α/β/γ-peptides) on the... 
MEDICINAL CHEMISTRY | GAMMA | DESIGN | AMINO-ACIDS | SECONDARY STRUCTURES | FOLDAMERS | PROTEIN-PROTEIN INTERACTIONS | CHEMISTRY, MULTIDISCIPLINARY | HYBRID PEPTIDES | ALPHA-HELIX MIMICRY | BETA | Peptides - chemistry | Protein Structure, Secondary | Amino acids | Nuclear magnetic resonance | Structure | Analysis | Circular dichroism
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 02/2015, Volume 137, Issue 6, pp. 2183 - 2186
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 05/2011, Volume 133, Issue 19, pp. 7336 - 7339
Artificial mimicry of α-helices offers a basis for development of protein–protein interaction antagonists. Here we report a new type of unnatural peptidic... 
DESIGN | ACIDS | SECONDARY STRUCTURES | FOLDAMERS | CONSEQUENCES | BETA-PEPTIDE | CRYSTALLOGRAPHY | INHIBITORS | ANTAGONISTS | CHEMISTRY, MULTIDISCIPLINARY | FAMILY | Amino Acid Sequence | Biomimetics | Peptides - chemistry | Protein Structure, Secondary | Water - chemistry | Amino Acids - chemistry | Molecular Sequence Data | Circular Dichroism | Solutions - chemistry
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 11/2015, Volume 54, Issue 48, pp. 14336 - 14339
Journal Article