Examples of 'hydrophobic amino acids' in a sentence
Meaning of "hydrophobic amino acids"
hydrophobic amino acids: Refers to a group of amino acids that repel water and are typically found in the interior of proteins. These amino acids play a crucial role in protein structure and function
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hydrophobic amino acids
Combinations of hydrophobic amino acids can also be employed.
It is also possible to eliminate the hydrophobic amino acids.
Hydrophobic amino acids useful in the present invention.
Lysozyme contains both hydrophilic and hydrophobic amino acids.
A sequence of hydrophobic amino acids is found in the middle.
The steric binding sites are mostly lined by hydrophobic amino acids.
Hydrophobic amino acids are preferred.
Helices exposed on the surface have a lower proportion of hydrophobic amino acids.
A high number of hydrophobic amino acids in the center of the protein.
The resulting polymers are amphiphilic but are not modified by hydrophobic amino acids.
There are hydrophobic amino acids and hydrophilic amino acids in protein molecules.
Chymotrypsin showed the expected specificity for large hydrophobic amino acids.
Suitable hydrophobic amino acids can also include amino acid analogs.
Amino acids which include combinations of hydrophobic amino acids can also be employed.
Hydrophobic amino acids are those acids which show a preference for the nonpolar solvent.
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The protein will necessarily have both hydrophilic and hydrophobic amino acids.
This lectin contains hydrophobic amino acids and its activity is calcium dependent.
The leader sequence fragment typically encodes a signal peptide comprised of hydrophobic amino acids.
A putative signal peptide sequence of mostly hydrophobic amino acids follows the initiator methionine.
Preferably, the polyepitopic regions defined above have the characteristic of containing hydrophobic amino acids.
This leader sequence consists of typical hydrophobic amino acids and ends at a plausible scission point.
Examples of amino acids include, but are not limited to hydrophobic amino acids.
A fraction without bitter hydrophobic amino acids will in particular be preferred for foods for humans.
With the exception of tyrosine, using titration to differentiate between hydrophobic amino acids is problematic.
Both Ile and Phe are hydrophobic amino acids and undergo analogous binding to neurophysins.
Suitable amino acids include naturally occurring and non-naturaty occurring hydrophobic amino acids.
The signal peptide usually contains a series of hydrophobic amino acids adopting a secondary alpha helix structure.
Suitable amino acids include naturally occurring and non-naturally occurring hydrophobic amino acids.
Medium sized hydrophobic amino acids Leu and Ile are well accepted in all DR alleles.
In certain embodiments, the flanking hydrophobic amino acids are the same.
The hydrophobic amino acids specified above may work as foam inhibitors for saccharides-containing dry compositions.
With the intention of improving solubility ( replacement of hydrophobic amino acids with hydrophilic amino acids ).
It consists of 19 hydrophobic amino acids bordered by three upstream lysine residues.
The self-assembling peptides may be amphiphilic, alternating between hydrophobic amino acids and hydrophilic amino acids.
Examples of suitable hydrophobic amino acids include valine, leucine, and isoleucine.
The protease cleaves human insulin at the C-terminal side of hydrophobic amino acids.
The C-terminus is composed of hydrophobic amino acids that stay inserted in the ER membrane.
In a preferred embodiment of the present invention C is 3 or 4 hydrophobic amino acids.
TABLE 3 Hydrophobic amino acids useful in the.
Both D, L and racemic configurations of hydrophobic amino acids can be employed.
Large non-polar, hydrophobic amino acids include phenylalanine, tryptophan and tyrosine.
The signal peptide ( sp ) is typically rich in hydrophobic amino acids.
Exemplified hydrophobic amino acids include valine, leucine, isoleucine, methionine, phenylalanine, and tryptophan.
It is also preferred that the number of hydrophobic amino acids is 7 or 8.
Preferred hydrophobic amino acids include leucine, isoleucine, alanine, valine, phenylalanine and glycine.
The third domain is the transmembrane domain, a stretch of approx . 20 hydrophobic amino acids.
Non-naturally-occurring hydrophobic amino acids also are included.
A therapeutic composition as claimed in claim 1 in which E is 1 to 3 hydrophobic amino acids.
These additives include hydrophobic amino acids such as tryptophan, tyrosine, leucine, phenylalanine, and the like.
A secretory sequence usually comprises 15 to 35 essentially hydrophobic amino acids.
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