Examples of 'a-helix' in a sentence
Meaning of "a-helix"
a-helix (noun) - in biochemistry, a common structural motif in proteins, characterized by a right-handed coiled shape resembling a helix
How to use "a-helix" in a sentence
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a-helix
The stability of the a-helix is increased upon complex formation.
The peptidomimetic macrocycle comprises at least one a-helix motif.
The transition from a-helix to random coil occurs within a narrow pH.
In some embodiments, the peptidomimetic macrocycle comprises at least one a-helix motif.
This substitution results in a stabilization of an a-helix in the receptor-binding region of the hormone.
Circular dichroism may conveniently be used to test for the presence of an a-helix.
A certain length of a-helix appears necessary to bridge the distance between the two sites.
The stable secondary structure can comprise at least two a-helix structures.
Between these two a-helix domains there is the immunodominant domain including a small loop.
From the score, the probability of the sequence being a membrane spanning a-helix is given.
Serum albumin is predominantly a-helix with three structural domains, each subdivided into two subdomains.
In particular embodiments, the stable secondary structure comprises at least two a-helix structures.
There is also no a-helix in the hAR LBD model in this área.
The peptidomimetic macrocycle resulting from a method of the invention comprises a-helix in aqueous solution.
It has been reported that a-helix 1 of Domain I is removed following receptor binding.
See also
Structural analysis of the amino acid sequences in this region strongly predicts an amphipathic a-helix.
In some embodiments, the macrocycle-forming linker stabilizes an a-helix motif included within the peptidomimetic macrocycle.
This has been achieved by optimizing the hydrophilic and hydrophobic faces of the modeled a-helix.
Mitogenicity can be affected by mutations in the N terminal a-helix and changes to sulfhydryl groups.
Indicates that the secondary structure in TFE has converted from B-Sheet to a-helix.
Domain I is a bundle of seven alpha helices where a-helix 5 is surrounded by six amphipathic helices.
This confirms the calculation of secondary structure components, which suggests a marginal number of a-helix elements.
The polypeptide may comprise an EF a-helix located on the EF chain.
According to an advantageous aspect, said GAG binding region is a C terminal a-helix.
The parameters of the a-helix structure are the following,.
Lipid affinity, A measurement of the relative binding affinity of an amphipathic a-helix for lipids.
The a-helix bundle pore includes a pore that is formed by a-helices.
A dodecapeptide motif is located at the C-terminal end of the first a-helix in each domain.
The a-helix is more stable than an a-helix of a corresponding non-macrocyclic polypeptide ;.
It is therefore estimable that the secondary structure of the CSF contains an a-helix structure.
In a particular embodiment, the helix is an a-helix according to Schiffer-Edmundson's wheel representation.
In some embodiments, the peptidomimetic macrocycle comprises an a-helix.
The fusogenic agent may have an a-helix structure, for example.
The two a-helix containing domains are arranged in very stable six-helix bundles.
The stipled cylinder represents the a-helix II region.
In other embodiments, the a-helix is more stable than an a-helix of a corresponding non-macrocyclic polypeptide.
The peptidomimetic macrocycle comprises an a-helix in aqueous solution ;.
This secondary structure is also sometimes called a classic Pauling-Corey-Branson a-helix.
Specifically, polypeptide is preferable, and a-helix polypeptide and the like are more preferable, for example.
A product according to any of claims 1-6 wherein the protein comprises a a-helix structure.
The a-helix and the B-strand are elements of secondary structure.
The compound of claim 1, wherein the compound comprises an a-helix in aqueous solution.
Formation of an a-helix typically results in an upfield ( negative ) shift for the Ha resonance.
Also, a wrong-handed amino acid disrupts the stabilizing a-helix in proteins.
The role of helix dipoles in stabilizing a-helix formation has been explored ( Marcuse and Baldwin ).
The peptidomimetic macrocycle of claim 1 wherein the peptidomimetic macrocycle comprises an a-helix and,.
The barrel is preceded by a short a-helix and by a flexible N-terminal tail.
In some embodiments, the macrocycle-forming linker spans approximately 1 turn of the a-helix.
This N-terminal presequence often contains an a-helix and several basic residues.
In other embodiments, the macrocycle-forming linker spans approximately 2 turns of the a-helix.
