Cell life depends on the dynamics of molecular processes: molecule folding, organelle building and transformations involving membrane fusion, protein activation and degradation. To carry out these processes, the hydrophilic/hydrophobic interfaces of amphipathic systems such as membranes and native proteins must be disrupted. In the past decade, protein fragments acting in the disruption of interfaces have been evidenced: they are named the tilted or oblique peptides. Due to a peculiar distribution of hydrophobicity, they can disrupt hydrophobicity interfaces. Tilted peptides should be present in many proteins involved in various stages of cell life. This hypothesis overviews their ...
AbstractResearch on antimicrobial peptides is in part driven by urgent medical needs such as the ste...
AbstractHydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the appar...
At physiological conditions, most proteins or peptides can fold into relatively stable structures th...
peer reviewedCell life depends on the dynamics of molecular processes: molecule folding, orga...
Tilted peptides are short sequence fragments (10-20 residues long) that possess an asymmetric...
Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution ...
AbstractPhysical properties of membranes, such as fluidity, charge or curvature influence their func...
Various peptide segments have been modeled as asymmetric amphipathic alpha-helices. Theoretical calc...
This review describes a class of peptides that associate with lipids in membranes and are com...
The Chameleon peptide (Chain) is a peptide designed from two regions of the GB1 protein, one folded ...
The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1 protein, one f...
In this review we discuss recent insights obtained from well-characterized model systems into the fa...
A class of peptides that associate with lipids, known as oblique-orientated peptides, was rec...
A diverse range of biologically critical phenomena involve membrane remodeling and/or the induction ...
Here, we predicted the minimal N-terminal fragment of gp41 required to induce significant mem...
AbstractResearch on antimicrobial peptides is in part driven by urgent medical needs such as the ste...
AbstractHydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the appar...
At physiological conditions, most proteins or peptides can fold into relatively stable structures th...
peer reviewedCell life depends on the dynamics of molecular processes: molecule folding, orga...
Tilted peptides are short sequence fragments (10-20 residues long) that possess an asymmetric...
Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution ...
AbstractPhysical properties of membranes, such as fluidity, charge or curvature influence their func...
Various peptide segments have been modeled as asymmetric amphipathic alpha-helices. Theoretical calc...
This review describes a class of peptides that associate with lipids in membranes and are com...
The Chameleon peptide (Chain) is a peptide designed from two regions of the GB1 protein, one folded ...
The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1 protein, one f...
In this review we discuss recent insights obtained from well-characterized model systems into the fa...
A class of peptides that associate with lipids, known as oblique-orientated peptides, was rec...
A diverse range of biologically critical phenomena involve membrane remodeling and/or the induction ...
Here, we predicted the minimal N-terminal fragment of gp41 required to induce significant mem...
AbstractResearch on antimicrobial peptides is in part driven by urgent medical needs such as the ste...
AbstractHydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the appar...
At physiological conditions, most proteins or peptides can fold into relatively stable structures th...