Search results
Results from the WOW.Com Content Network
At high concentrations of guanidinium chloride (e.g., 6 M), proteins lose their ordered structure, and they tend to become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations in the millimolar range in vivo, guanidinium chloride has been shown to "cure" prion positive yeast cells (i.e. cells exhibiting a ...
The general structure of a guanidine. Guanidines are a group of organic compounds sharing a common functional group with the general structure (R 1 R 2 N)(R 3 R 4 N)C=N−R 5. The central bond within this group is that of an imine, and the group is related structurally to amidines and ureas.
Print/export Download as PDF; Printable version; ... Help. The general structure of a guanidine Subcategories. This category has the following 8 subcategories, out of ...
The following other wikis use this file: Usage on az.wikipedia.org Quanidin; Usage on bn.wikipedia.org গুয়ানিডিন; Usage on ca.wikipedia.org
Molecular structure diagrams used in drug-related pharmacology articles should be created using a molecule editor program, such as ChemDraw, ChemSketch, or ISIS/Draw (ChemDraw and Isis/draw are commercial software packages, ChemSketch is freeware.
It involves the reaction of an unprotected peptide thioester with a second, unprotected peptide that has an N-terminal cysteine residue. It is carried out in aqueous solution at neutral pH, usually in 6 M guanidine.hydrochloride, in the presence of an arylthiol catalyst and typically gives near-quantitative yields of the desired ligation product.
Guanidine is a special case of a species that is exceptionally stable when protonated, analogously to the reason that makes perchloric acid and sulfuric acid very strong acids. Acids with a p K a of more than about 13 are considered very weak, and their conjugate bases are strong bases.
The order of the tendency of ions to make or break water structure is the basis of the Hofmeister series. Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and, as it was discovered later, on the stability of their secondary and tertiary structures .