These results suggest that alpha-catenin is composed of repeating antiparallel helical domains.
2
It is composed of a short alpha-helix and a three-stranded antiparallel beta-sheet.
3
The molecule consists of a typical four-helix antiparallel bundle with overhand connection.
4
In contrast, the stability of the antiparallel complex is not salt-dependent.
5
We also studied antiparallel GQ models with alternative syn-anti patterns of the G-quartets.
6
The structure is comprised of a central antiparallel beta-sheet flanked on both sides by alpha-helices.
7
We have substituted an antiparallel heterodimeric coiled-coil motif for the β-strand stalk in this antibody.
8
From these data, it is apparent that self-assembly involves the formation of antiparallel beta-sheets and pi-pi-stacking.
9
The two GAT domains are connected by an antiparallel coiled coil, forming a 90 A-long barbell-like structure.
10
Thus, triplexforming antiparallel purine-hairpins can be a potentially useful strategy for both single-strand and double-strand nucleic acid recognition.
11
This interaction mode contrasts with those typically driving squaramide-based assemblies based on either hydrogen bonds or antiparallel stacking.
12
The secondary structure contains one alpha-helix and eight beta-strands, seven of which are arranged in two contiguous, antiparallel beta-sheets.
13
Here we show that the approach can be generalized to obtain antiparallel and parallel dimers as well as trimer motifs.
14
Here we report a long-range antisymmetric interlayer exchange interaction in perpendicularly magnetized synthetic antiferromagnets with parallel and antiparallel magnetization alignments.
15
The protein contains one alpha-helix and two strands of antiparallel beta-sheet, with a type IV beta-turn connecting the two strands.
16
We found that replacement of an interhelical salt bridge with a covalent bond can stabilize antiparallel motifs in short sequences.