Bridge

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Bridge

1. In broadcasting, a fade-out between two scenes indicating a transition.

2. An advertisement in a magazine or other periodical that goes across two pages.

References in periodicals archive ?

04 A) and subsequent formation of disulfide bridges make greater changes in the structure of the molecule than incorporation of glutathione.

Basal Glutathionylation of Na,K-ATPase [alpha]-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis

The [alpha]-subunit composed of 92 amino acids linked by five disulfide bridges is common to all members of the glycoprotein-hormone family.

Human chorionic gonadotropin (hCG) testing--Part I

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.

Scientists discover first protein-based amphibian toxin in Chinese tree frog

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

MS sequencing techniques: Dr Fiona Greer, director biochemical services, at M-Scan discusses the analytical characterization of biopharmaceutical products using mass spectrometry

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 (Figure 3).

Genetic divergence and dispersal of yellow fever virus, Brazil

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.

Syneresis in rennet gels

The UV light is absorbed by the amino acid tryptophan, which breaks the disulfide bridges holding parts of the antibody together and causes a particular part of the amino acid cysteine, called a thiol group, to become exposed at the tail end of the antibody.

Monthly Tip Sheet: Research Highlights from Biomedical Optics Express - October 2011

This peptide mapping philosophy can even be extended to determine the location of the disulfide bridges.

Critical steps for biosimilar assessment: establishing "finger-print like" biosimilarity prior to the clinic