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A Concise Route to Valacyclovir Hydrochloride

Helvetica chimica acta, 2011-04, Vol.94 (4), p.592-596

2011

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Synthesis, and Helix or Hairpin-Turn Secondary Structures of 'Mixed' α/β-Peptides Consisting of Residues with Proteinogenic Side Chains and of 2-Amino-2-methylpropanoic Acid (Aib)

Helvetica chimica acta, 2006-09, Vol.89 (9), p.1801-1825

2006

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Note: Helix or No Helix of β-Peptides Containing β3hAla(αF) Residues?

Helvetica chimica acta, 2011-03, Vol.94 (3), p.355-361

2011

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Note: Helix or No Helix of β ‐Peptides Containing β 3 hAla( α F) Residues?

Helvetica chimica acta, 2011-03, Vol.94 (3), p.355-361

2011

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β-Peptide Conjugates: Syntheses and CD and NMR Investigations of β/α-Chimeric Peptides, of a DPA-β-Decapeptide, and of a PEGylated β-Heptapeptide

Helvetica chimica acta, 2009-12, Vol.92 (12), p.2698-2721

2009

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β-Peptidic Secondary Structures Fortified and Enforced by Zn2+ Complexation – On the Way toβ-Peptidic Zinc Fingers?

Helvetica chimica acta, 2006-03, Vol.89 (3), p.361-403

2006

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NMR‐Solution Structures of Fluoro‐Substituted β ‐Peptides: A 3 14 ‐Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in an α ‐Fluoro‐Amide Group

Helvetica chimica acta, 2007-12, Vol.90 (12), p.2251-2273

2007

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The Effect of Backbone-Heteroatom Substitution on the Folding of Peptides - A Single Fluorine Substituent Prevents a?-Heptapeptide from Folding into a314-Helix (NMR Analysis)

Helvetica chimica acta, 2005-02, Vol.88 (2), p.266-280

2005

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The Effect of Backbone-Heteroatom Substitution on the Folding of Peptides - A Single Fluorine Substituent Prevents a β-Heptapeptide from Folding into a 314-Helix (NMR Analysis)

Helvetica chimica acta, 2005-02, Vol.88 (2), p.266-280

2005

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New Open‐Chain and Cyclic Tetrapeptides, Consisting of α ‐, β 2 ‐, and β 3 ‐Amino‐Acid Residues, as Somatostatin Mimics – A Survey

Helvetica chimica acta, 2008-09, Vol.91 (9), p.1736-1786

2008

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New Open-Chain and Cyclic Tetrapeptides, Consisting of α-, β2-, and β3-Amino-Acid Residues, as Somatostatin Mimics - A Survey

Helvetica chimica acta, 2008-09, Vol.91 (9), p.1736-1786

2008

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β-Peptidic Secondary Structures Fortified and Enforced by Zn2+ Complexation - On the Way to β-Peptidic Zinc Fingers?

Helvetica chimica acta, 2006-03, Vol.89 (3), p.361-403

2006

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NMR-Solution Structures of Fluoro-Substituted β-Peptides: A 314-Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in an α-Fluoro-Amide Group

Helvetica chimica acta, 2007-12, Vol.90 (12), p.2251-2273

2007

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NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains

Helvetica chimica acta, 2005-07, Vol.88 (7), p.1969-1982

2005

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NMR‐Solution Structures in Methanol of an α ‐Heptapeptide, of a β 3 / β 2 ‐Nonapeptide, and of an all‐ β 3 ‐Icosapeptide Carrying the 20 Proteinogenic Side Chains

Helvetica chimica acta, 2005-07, Vol.88 (7), p.1969-1982

2005

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A Concise Route to Valacyclovir Hydrochloride

Synthesis, and Helix or Hairpin-Turn Secondary Structures of 'Mixed' α/β-Peptides Consisting of Residues with Proteinogenic Side Chains and of 2-Amino-2-methylpropanoic Acid (Aib)

Note: Helix or No Helix of β-Peptides Containing β3hAla(αF) Residues?

Note: Helix or No Helix of β ‐Peptides Containing β 3 hAla( α F) Residues?

β-Peptide Conjugates: Syntheses and CD and NMR Investigations of β/α-Chimeric Peptides, of a DPA-β-Decapeptide, and of a PEGylated β-Heptapeptide

β-Peptidic Secondary Structures Fortified and Enforced by Zn2+ Complexation – On the Way toβ-Peptidic Zinc Fingers?

NMR‐Solution Structures of Fluoro‐Substituted β ‐Peptides: A 3 14 ‐Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in an α ‐Fluoro‐Amide Group

The Effect of Backbone-Heteroatom Substitution on the Folding of Peptides - A Single Fluorine Substituent Prevents a?-Heptapeptide from Folding into a314-Helix (NMR Analysis)

The Effect of Backbone-Heteroatom Substitution on the Folding of Peptides - A Single Fluorine Substituent Prevents a β-Heptapeptide from Folding into a 314-Helix (NMR Analysis)

New Open‐Chain and Cyclic Tetrapeptides, Consisting of α ‐, β 2 ‐, and β 3 ‐Amino‐Acid Residues, as Somatostatin Mimics – A Survey

New Open-Chain and Cyclic Tetrapeptides, Consisting of α-, β2-, and β3-Amino-Acid Residues, as Somatostatin Mimics - A Survey

β-Peptidic Secondary Structures Fortified and Enforced by Zn2+ Complexation - On the Way to β-Peptidic Zinc Fingers?

NMR-Solution Structures of Fluoro-Substituted β-Peptides: A 314-Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in an α-Fluoro-Amide Group

NMR-Solution Structures in Methanol of an α-Heptapeptide, of a β3/β2-Nonapeptide, and of an all-β3-Icosapeptide Carrying the 20 Proteinogenic Side Chains

NMR‐Solution Structures in Methanol of an α ‐Heptapeptide, of a β 3 / β 2 ‐Nonapeptide, and of an all‐ β 3 ‐Icosapeptide Carrying the 20 Proteinogenic Side Chains

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