English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

The interaction of the myelin basic protein and two peptides derived from it with the anionic detergent SDS (sodium dodecyl sulphate) was studied. At molar ratios of detergent/protein of up to approx. 20:1 the transient increase in turbidity (as measured by increases in A230) is proportional to the ratio. Between ratios of 30:1 and 100:1 the effect of the detergent is constant and maximal. At molar ratios exceeding 100:1 the transient increase in turbidity decreases with increasing amounts of detergent. With increasing ionic strength the rapid development of turbidity is inhibited, whereas the slow decay of turbidity is not affected. Neither of the peptide fragments produced by cleavage of the myelin basic protein at the single tryptophan residue, nor both when mixed, produce measurable turbidity when mixed with SDS. Under similar conditions poly-L-lysine of similar molecular size to the basic protein shows the increase in turbidity but not the decay. The interaction between the protein and SDS is interpreted in molecular terms, which involve the initial ionic interaction of the detergent with protein resulting in aggregation and turbidity in the solution. Within the aggregated complexes molecules rearrange to maximize hydrophobic interactions.

Interaction of the myelin basic protein with the anionic detergent sodium dodecyl sulphate