Examples of 'cys residues' in a sentence
Meaning of "cys residues"
Cys residues refers to the amino acid cysteine residues in a protein sequence. Cysteine is an important amino acid that contains a sulfur atom, which can form disulfide bonds with other cysteine residues. These bonds play a crucial role in the stabilization and folding of proteins, as well as in various biological processes. The term 'cys residues' is commonly used in the field of biochemistry and molecular biology when analyzing protein structures and functions
How to use "cys residues" in a sentence
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cys residues
Cys residues can not be identified by protein microsequencing.
The positions of the four Cys residues are shown.
Cys residues were included in the linear peptides to enable their cyclization.
This generated free Cys residues in half of the molecules.
The Cys residues were used to assist in coupling to a protein carrier as described below.
The protection of at least one of the Cys residues by an acetamidomethyl group.
The two Cys residues are joined by a disulfide bond.
The substitution of at least one of the Cys residues by a Ser residue.
The conserved Cys residues are enclosed in yellow boxes.
The substitution of at least one of the Cys residues by an Ala residue.
Several Cys residues have been identified as being sensitive to redox changes.
The substitution of at least one of the Cys residues by a gamma aminobutyric acid residue.
The two Cys residues are joined by a disulfide bond in the active compounds.
Chimeras with other conotoxins may include additional Cys residues and additional disulphide bonds.
Four His and Cys residues are used to bind a metal ion in a tetrahedral geometry.
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Preferably cyclic conotoxin peptides will retain the Cys residues and characteristic disulphide bonding pattern.
Such Cys residues are spaced apart from each other by a number of intermittent amino acids.
The term octreotide derivatives includes those including the moiety having a bridge between the Cys residues.
Four of the six Cys residues in spHAS are conserved with seHAs.
In a preferred method of alignment, Cys residues are aligned.
Disulfide bonds between Cys residues can be formed using dimethyl sulfoxide Tam et al.
A peptide of this invention preferably has 4 Cys residues.
Even free internal Cys residues may be present in either of the reacting segments.
Cyclization vÃa formation of S-S bonds through incorporation of two Cys residues is also possible.
The Cys residues are bold and underlined and the predicted transmembrane region is boxed.
In an alternative embodiment, the two Cys residues form an intermolecular disulphide bond.
The Cys residues are the best-conserved feature.
In the amatoxins, this is formed as a sulfoxide bridge between the Trp and Cys residues.
The distribution of Cys residues is conserved among ALB family members.
The peptides of the invention, like the bacterial ST peptides, have six Cys residues.
The positions of AFM Cys residues are clearly consistent with this arrangement FIG.
The extracellular domain contains four potential N-glycosylation sites and three Cys residues.
Non-canonical Cys residues were marked by dots.
Cys residues are then targeted by several posttranslational redox modifications including S-glutathionylation.
Alternatively, the internal Cys residues or Cys residues on a linker can be used.
Cys residues at positions 67 and 81 may also form structurally important disulphide bonds.
However, antibody molecules have Cys residues which form intra - and interchain disulfide bridges.
The first disulphide bridge was formed between unprotected Cys residues using K3Fe ( CN ) 6.
The 2 Cys residues are linked to each other by a disulfide bridge.
Pramlintide has a disulfide bridge between the two Cys residues and a C-terminal amide group.
At least one of the Cys residues is substituted with Ser ; and combinations thereof.
Protein S-glutathionylation is reversible and protects Cys residues from overoxidation by ROS.
The relatively high number of Cys residues offers a variety of inter - and intramolecular crosslinking possibilities.
More advantageously, a disulfide linkage is also present between the two Cys residues at positions 4 and 21.
All three Cys residues in the mouse IgG2a hinge are used for inter-heavy chain disulfides.
Da if containing 3 free Cys residues.
Two of the 6 Cys residues in spHAS are conserved and identical in HAS1 and HAS2.
The charge on the Zn metal ion ( M ) is neutralized by the two Cys residues.
Human CD40-L comprises five Cys residues in its extracellular domain.
Forming the disulfide B-strand linkage between the side-chains of the Cys residues in positions 4 and 11 ;.
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