Examples of 'α-helices' in a sentence
Meaning of "α-helices"
α-helices (noun) - In biology and chemistry, α-helices are a common structural motif in proteins. They are formed by a right-handed coiled or spiral shape of a polypeptide chain. α-helices play a crucial role in protein folding and are significant elements in the secondary structure of proteins
How to use "α-helices" in a sentence
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α-helices
The motif is characterized by two α-helices connected by a loop.
Aquaporin proteins are composed of a bundle of six transmembrane α-helices.
Calponin is mainly made up of α-helices with hydrogen bond turns.
It is evident that the predicted protein structure is vastly composed of α-helices.
The hydrophobic interactions between these α-helices stabilize dimerization.
Their membrane-anchoring α-helices have been removed to facilitate the extraction and crystallization.
MetJ interacts with DNA bases via a pair of α-helices.
There are also seven additional α-helices that are not part of the barrel.
It operates similarly to formaldehyde, causing the deformation of proteins ' α-helices.
Rotation and tilting of transmembrane α-helices may both contribute to these conformational changes.
There are two main types of secondary structure, α-helices and β-sheets.
In the complex, two α-helices from each subunit come together to form a four-helix bundle.
The domain is believed to be made up of a β-pleated sheet and two α-helices.
These residues are folded into six α-helices and five β-strands.
The core of the enzyme consists of a five-stranded mixed β-sheet flanked by α-helices.
See also
The parallel β-strands and α-helices form the inner and outer wall of the horseshoe, respectively.
Bcl-2 family proteins have a general structure that consists of a hydrophobic α-helix surrounded by amphipathic α-helices.
Structure = = The motif is characterized by two α-helices connected by a loop.
The four-α-helix bundle family, member cytokines have three-dimensional structures with a bundle of four α-helices.
The region is located in α-helices I, II, and the connecting band.
The 2nd NTD is a folded domain composed of three α-helices.
The α-helices may be parallel or anti-parallel, and usually adopt a left-handed super-coil Figure 1.
UDG is made of a four-stranded parallel β-sheet surrounded by eight α-helices.
The smaller N-terminal domain consists of three α-helices and four β-sheets.
The structure of RNase H commonly consists of a 5-stranded β-sheet surrounded by a distribution of α-helices.
Structurally, the KIX domain is a globular domain consisting of three α-helices and two short 310-helices.
All typically have three β-sheets ( named A, B and C ) and eight or nine α-helices named hA-hI.
