2024年12月12日 · We found that the 1 st and 7 th linkers maintain hydrogen bonds with the linked coiled-coil terminal residues, while the 4 th linker exhibits a more pronounced conformational change. In the snapshot at 500 ns, L4 leaves the vertex position and bends to the edge formed by the 2 nd and 8 th coiled coil.

A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands of a rope. ( Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions. [ 2 ]

We have designed a 2-stranded 44-residue coiled-coil protein (P44) consisting of 2 22-residue alpha-helices linked by 2 terminal disulfide groups to test whether the disulfide bridges could stabilize a 3-heptad coiled coil.

2023年4月1日 · α-Helix and coiled-coil geometry. A, the α helix has a rise per residue (r) of 1.5 Å, 3.6 residues per helical turn, a backbone radius of 2.3 Å, and is stabilized by i CO to i + 4 NH hydrogen bonds. B, in Crick’s helical nets, the positions of the Cα atoms of an α helix, are projected as points onto a 2D plot (red).

2020年3月2日 · Specifically, a symbiotic relationship between a hydrated alanine layer and metal-binding ligands can potentially lead to new hydrogen-bonding interactions that stabilize the system. We will show...

The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to …

Three stabilizing interactions have been identified: a unique hydrogen bonding–electrostatic network not previously observed in coiled-coils, and two other hydrophobic interactions involving leucine residues at positions e and g from both g-a‘ and d-e‘ interchain interactions with the hydrophobic core.

2016年1月15日 · The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

2016年5月6日 · Coiled-coil packing and oligomerization state are largely determined by position-specific identities of nonpolar residues that pack between the helices (20–22); salt bridge and hydrogen-bonding interactions between residues on the periphery can provide additional specificity (23–25).

2016年1月15日 · The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.