The occurrence of an eight-residue long segment of polypeptide chain in collagen helical conformation has been detected in bacteriochlorophyll a-protein by the application of an algorithm for identifying secondary structures in globular proteins from their $\alpha$-carbon positions. This segment spans residues 277 to 284 of the protein and is the longest known stretch of collagen helix to be observed in globular proteins
A method to identify β-sheets in globular proteins from extended strands, using only α-carbon posi...
This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, firs...
This year marks the 50th anniversary of the coiled?–?coil triple helical structure of collagen, firs...
The occurrence of an eight-residue long segment of polypeptide chain in collagen helical conformatio...
A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a ?-tur...
A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-tur...
Elucidation of the detailed structural features and sequence requirements for iv helices of various ...
Elucidation of the detailed structural features and sequence requirements for alpha helices of vario...
Elucidation of the detailed structural features and sequence requirements for α helices of various l...
A simple algorithm has been developed to detect β-bends and 'loops'-chain reversals containing five ...
An arrangement of three non-coaxial helical chains linked to one another by hydrogen bonds approxima...
The paper reports the details of the revised structure of collagen. It is composed of three helical ...
AbstractUnderstanding the sequence-structure relationships in globular proteins is important for rel...
The triple-helix is a unique secondary structural motif found primarily within the collagens. In col...
In the immediately preceding papers we have described several hydrogen-bonded planar-amide configura...
A method to identify β-sheets in globular proteins from extended strands, using only α-carbon posi...
This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, firs...
This year marks the 50th anniversary of the coiled?–?coil triple helical structure of collagen, firs...
The occurrence of an eight-residue long segment of polypeptide chain in collagen helical conformatio...
A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a ?-tur...
A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-tur...
Elucidation of the detailed structural features and sequence requirements for iv helices of various ...
Elucidation of the detailed structural features and sequence requirements for alpha helices of vario...
Elucidation of the detailed structural features and sequence requirements for α helices of various l...
A simple algorithm has been developed to detect β-bends and 'loops'-chain reversals containing five ...
An arrangement of three non-coaxial helical chains linked to one another by hydrogen bonds approxima...
The paper reports the details of the revised structure of collagen. It is composed of three helical ...
AbstractUnderstanding the sequence-structure relationships in globular proteins is important for rel...
The triple-helix is a unique secondary structural motif found primarily within the collagens. In col...
In the immediately preceding papers we have described several hydrogen-bonded planar-amide configura...
A method to identify β-sheets in globular proteins from extended strands, using only α-carbon posi...
This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, firs...
This year marks the 50th anniversary of the coiled?–?coil triple helical structure of collagen, firs...