The first crystal structure of an oligoproline adopting an all-trans polyproline II (PPII) helix is presented. The high-resolution structure provides detailed insight into the dimensions and conformational properties of oligoprolines that are important for, e.g., their use as "molecular rulers" and "molecular scaffolds". The structure also showed that the amides interact with each other within a PPII helix and that water is not necessary for PPII helicity
The proline analogue (2S,3aS,7aS)-octahydroindole-2-carboxylic acid (Oic) has been previously applie...
ABSTRACT: The importance of the left-handed polyproline II (PPII) helical conformation has recently ...
The polyproline II (PPII) conformation of protein backbone is an important secondary structure type....
The first crystal structure of an oligoproline adopting an <i>all-trans</i> polyproline II (PPII) he...
About half of the globular proteins are composed of regular secondary structures, alpha-helices, and...
International audienceAbout half of the globular proteins are composed of regular secondary structur...
The synthesis, structural properties, and folding patterns of a series of L-proline methanologues re...
Oligoprolines are commonly used as molecular scaffolds. Past studies on the persistence length of th...
In the last years polyproline II (PPII) structure has been demonstrated to be essential to biologica...
Left-handed polyproline II helices (PPII) are contiguous elements of protein secondary structure in ...
The left-handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is rema...
The left-handed polyproline II helix (PPII) is believed to be the preferred conformation for proline...
International audienceThe de novo design and synthesis of large and well-organized, tertiary-like, α...
PolyProline-II (PPII) helices are defined as a continuous stretch of a protein chain in which the co...
The polyproline type II (PPII) helix is a prevalent conformation in both folded and unfolded protein...
The proline analogue (2S,3aS,7aS)-octahydroindole-2-carboxylic acid (Oic) has been previously applie...
ABSTRACT: The importance of the left-handed polyproline II (PPII) helical conformation has recently ...
The polyproline II (PPII) conformation of protein backbone is an important secondary structure type....
The first crystal structure of an oligoproline adopting an <i>all-trans</i> polyproline II (PPII) he...
About half of the globular proteins are composed of regular secondary structures, alpha-helices, and...
International audienceAbout half of the globular proteins are composed of regular secondary structur...
The synthesis, structural properties, and folding patterns of a series of L-proline methanologues re...
Oligoprolines are commonly used as molecular scaffolds. Past studies on the persistence length of th...
In the last years polyproline II (PPII) structure has been demonstrated to be essential to biologica...
Left-handed polyproline II helices (PPII) are contiguous elements of protein secondary structure in ...
The left-handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is rema...
The left-handed polyproline II helix (PPII) is believed to be the preferred conformation for proline...
International audienceThe de novo design and synthesis of large and well-organized, tertiary-like, α...
PolyProline-II (PPII) helices are defined as a continuous stretch of a protein chain in which the co...
The polyproline type II (PPII) helix is a prevalent conformation in both folded and unfolded protein...
The proline analogue (2S,3aS,7aS)-octahydroindole-2-carboxylic acid (Oic) has been previously applie...
ABSTRACT: The importance of the left-handed polyproline II (PPII) helical conformation has recently ...
The polyproline II (PPII) conformation of protein backbone is an important secondary structure type....