Add to ORKGThe assembly of helical and β-sheet peptide blocks containing reactive chain ends results inhighly branched chain architectures (‘locked-in folds') mimicking native tertiary structures.This molecular kit strategy allows to bypass the protein folding problem in protein de novodesign and gives access to protein mimetics of high thermodynamic stability. The validity ofthis concept is exemplified for the design and synthesis of locked-in folds mimicking the zincfinger and MHC folding motif
AbstractBackground: Few examples exist of peptides of < 35 residues that form a stable tertiary stru...
The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a c...
Helical secondary and tertiary motifs are commonly observed as binding epitopes in natural and engin...
Summary: The assembly of helical and β-sheet peptide blocks containing reactive chain ends results i...
The ultimate goal in protein de novo design is the construction of artificial proteins exhibiting ta...
A symposium report. The concept of template assembled synthetic proteins (TASP) has been evaluated f...
An iterative design process involving the synthesis and structural analyses of five polypeptides pat...
Design of foldamers, unnatural backbone oligomers that mimic the structure of proteins, is an import...
Proteins play key roles in biological processes that are highly dependent on their three-dimensional...
International audienceA number of foldamer backbones have been described as useful mimics of protein...
The rational design of peptides that fold to form discrete nanoscale objects, and/or self-assemble i...
A number of foldamer backbones have been described as useful mimics of protein secondary structure e...
AbstractThe design of proteins with tailored functions remains a relatively elusive goal. Small size...
Background: An attempt is being made to produce two-helix bundles that are soluble in apolar media, ...
The folding of natural proteins typically relies on hydrophobic packing, metal binding, or disulfide...
AbstractBackground: Few examples exist of peptides of < 35 residues that form a stable tertiary stru...
The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a c...
Helical secondary and tertiary motifs are commonly observed as binding epitopes in natural and engin...
Summary: The assembly of helical and β-sheet peptide blocks containing reactive chain ends results i...
The ultimate goal in protein de novo design is the construction of artificial proteins exhibiting ta...
A symposium report. The concept of template assembled synthetic proteins (TASP) has been evaluated f...
An iterative design process involving the synthesis and structural analyses of five polypeptides pat...
Design of foldamers, unnatural backbone oligomers that mimic the structure of proteins, is an import...
Proteins play key roles in biological processes that are highly dependent on their three-dimensional...
International audienceA number of foldamer backbones have been described as useful mimics of protein...
The rational design of peptides that fold to form discrete nanoscale objects, and/or self-assemble i...
A number of foldamer backbones have been described as useful mimics of protein secondary structure e...
AbstractThe design of proteins with tailored functions remains a relatively elusive goal. Small size...
Background: An attempt is being made to produce two-helix bundles that are soluble in apolar media, ...
The folding of natural proteins typically relies on hydrophobic packing, metal binding, or disulfide...
AbstractBackground: Few examples exist of peptides of < 35 residues that form a stable tertiary stru...
The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a c...
Helical secondary and tertiary motifs are commonly observed as binding epitopes in natural and engin...