Examples of 'alpha helix' in a sentence
Meaning of "alpha helix"
alpha helix: In biochemistry, an alpha helix is a common motif in protein structure where the protein chain is coiled like a spring
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- A secondary structure found in many proteins, in which the amino acids are arranged in a coil, or helix, with almost no free space on the inside and all side chains being pointed towards the outside
How to use "alpha helix" in a sentence
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alpha helix
Its structure comprises a single alpha helix.
Alpha helix mimetics and methods relating thereto.
Urocortin is composed of a single alpha helix structure.
This is typically an alpha helix comprising of several hydrophobic residues.
There is also a conserved alpha helix.
Neither part of an alpha helix nor a beta sheet structure.
It may comprise a hydrophobic alpha helix.
Alpha helix promoting amino acids are known in the art.
See the amphipathic nature of the alpha helix.
The alpha helix structure is an example of the secondary structure of proteins.
Modifications which achieve a stabilized alpha helix structure are described herein.
The region containing this amino acid corresponds to an alpha helix.
Transmembrane domains may be hydrophobic alpha helix that spans the cell membrane.
This amino acid is generally a leucine residue in the middle of an alpha helix.
The spherical core consists of an alpha helix and a beta sheet.
See also
An alpha helix is a motif of protein secondary structure, resembling a coiled conformation.
These had a value associated with the occurrence of the alpha helix structure.
Figure 1 shows an alpha helix from the side and top views.
Spectroscopic studies on insulin also indicate that moderate concentrations of alcohols enhance alpha helix content.
Also the third tryptophan in the third alpha helix is not always conservered.
The signal peptide usually contains a series of hydrophobic amino acids adopting a secondary alpha helix structure.
Such methods of metal binding-based alpha helix stabilization are known in the art.
Intramolecular bridges other than a lactam bridge can be used to stabilize the alpha helix of Q.
The bZIP domain contains an alpha helix with a leucine at every 7th amino acid.
To elaborate, the benign form of PrP shows a multiple alpha helix geometry.
Interestingly, an alpha helix is also predicted from the corresponding region of Vpx.
The transmembrane domain is typically a hydrophobic alpha helix that spans the membrane.
Scramblase proteins contain a region of conservation that possesses a 12-stranded beta barrel surrounding a central alpha helix.
At least four surface-exposed amino acids in the alpha helix or adjacent regions are modified.
Considering this fact, we propose a de novo method for the prediction of alpha helix.
This epitope is part of an extended alpha helix in the HA2 region.
Further, a part of the oxyntomodulin sequence may be substituted with a sequence stabilizing alpha helix.
The single alpha helix present on each of the 5 protomers is located on the A face.
This study stemmed from work on the research vessel Alpha Helix on the Amazon River.
For a discussion of alpha helix formers and breakers, see Chou and Fasman, supra.
In general, reduced solution polarity appears to favor formation of alpha helix in short peptides.
In some embodiments, the alpha helix promoting amino acid is AIB or Glu.
This included the structure of the most important chain - the alpha helix chain.
Additionally, the second alpha helix contains a unique leucine at position 17.
In one embodiment, the transmembrane domain is a hydrophobic alpha helix that spans the membrane.
The alpha helix is also called a classic Pauling-Corey-Branson α-helix.
Similarly, a linker may comprise a basic linker and a structural motif, such as an alpha helix.
In some aspects, the alpha helix stabilizing amino acid is located at position 16.
In certain embodiments, the transmembrane domain can be a hydrophobic alpha helix that spans the membrane.
The alpha helix of a polypeptide chain comprises an average of 3.6 residues per turn.
This secondary structure is also sometimes called a classic Pauling-Corey-Branson alpha helix see below.
Thus, it can form an alpha helix only in conjunction with the linker " termini ".
His work on keratin provided the foundation for Linus Pauling 's discovery of the alpha helix.
A short ( two to four turns ) N-terminal alpha helix is also present in most LSm proteins.
Finally, there is a unique leucine at position 17 in the second alpha helix.
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