Formation of disulfide bridges
can increase rigidity of the structure and prevent conformational lability of the molecule.
These values, derived from current commercial products, predicted to maintain biological, physicochemical, and structural integrity, can be used as a reference range, where the preservation of the folded structure inhibits the exposure of sulfhydryl groups and their oxidation to sulfenic, sulfinic, or sulfonic groups while restraining disulfide bridges
play a major role in stabilization, the folding process and so, existence of cysteine residues and disulfide bonding pattern were determined using DISULFIND server (9).
Purpose; Due to an antioxidant substrate, high proportions of reducible disulfide bridges
are typically for the viscotoxin 1-PS from Scots Pine (Pinus silvestris L.) mistletoe (Viscum album ssp.
The [alpha]-subunit composed of 92 amino acids linked by five disulfide bridges
is common to all members of the glycoprotein-hormone family.
In protein sequence and structure, anntoxin was very similar to dendrotoxins (the venoms found in cobras and other mamba snakes) and cone snail toxins, though anntoxin only has two disulfide bridges
(a strong link that helps keep proteins folded) compared to three in the other types.
In short, MS methods have the capability to provide molecular weight and sequence data, detect errors of translation from the gene sequence, identify post-translational modifications, identify sites of glycosylation (including carbohydrate structure and sequence), identify heterogeneity at the N- and C-termini and assign disulfide bridges
, among other things!
The fundamental pattern-recognition approach in TEXTAL is based on extracting numeric features that attempt to capture relevant information about local electron density for various purposes (such as identifying C[alpha] atoms, comparing side chains, or detecting disulfide bridges
Several members of the older Para subclade had one or more mutations within the fusion peptide region of the E protein, including substitutions that disrupted conserved disulfide bridges
Both a-lactalbumin and b-lactoglobulin can be extensively polymerized by transglutaminase when they are partly unfolded by the chemical reduction of the disulfide bridges
stabilizing their tertiary structure, or by performing the reaction at alkaline pH.
One way to do this is to take the antibody, reduce and protect the disulfide bridges
, and then cleave it into smaller pieces using a protease enzyme.