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An example of a double helix in molecular biology is the nucleic acid double helix. An example of a conic helix is the Corkscrew roller coaster at Cedar Point amusement park. Some curves found in nature consist of multiple helices of different handedness joined together by transitions known as tendril perversions.
Since the α-helix is defined by its hydrogen bonds and backbone conformation, the most detailed experimental evidence for α-helical structure comes from atomic-resolution X-ray crystallography such as the example shown at right. It is clear that all the backbone carbonyl oxygens point downward (toward the C-terminus) but splay out slightly ...
These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [ 17 ] [ 18 ] [ 19 ...
The tertiary arrangement of DNA's double helix in space includes B-DNA, A-DNA, and Z-DNA. Triple-stranded DNA structures have been demonstrated in repetitive polypurine:polypyrimidine Microsatellite sequences and Satellite DNA. B-DNA is the most common form of DNA in vivo and is a more narrow, elongated helix than A-DNA. Its wide major groove ...
The helix-loop-helix structure has two helices connected by a 'loop'. These are fairly common and usually bind ligands.For example, calcium binds with the carboxyl groups of the side chains within the loop region between the helices.
Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules, and dynein, which moves cargo inside cells towards the nucleus and produces the axonemal beating of motile cilia and flagella. "[I]n effect, the [motile cilium] is a ...
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A pi helix (or π-helix) is a type of secondary structure found in proteins. Discovered by crystallographer Barbara Low in 1952 [ 1 ] and once thought to be rare, short π-helices are found in 15% of known protein structures and are believed to be an evolutionary adaptation derived by the insertion of a single amino acid into an α-helix . [ 2 ]