Selective chemical protein modification

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Selective chemical protein modification.

Chemical modification of proteins is an important tool for probing natural systems, creating therapeutic conjugates and generating novel protein constructs. Site-selective reactions require exquisite control over both chemo- and regioselectivity, under ambient, aqueous conditions. There are now various methods for achieving selective modification of both natural and unnatural amino acids--each ...

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Olefin metathesis for site-selective protein modification.

For a reaction to be generally useful for protein modification, it must be site-selective and efficient under conditions compatible with proteins: aqueous media, low to ambient temperature, and at or near neutral pH. To engineer a reaction that satisfies these conditions is not a simple task. Olefin metathesis is one of most useful reactions for carbon-carbon bond formation, but does it fit the...

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Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping.

Aminoacetylation of lysine residues and the modification of arginine by 1,2-cyclohexanedione to N7,N8-(dihydroxy-1,2-cyclohexylidene)arginine were used for probing the surface topology of hen-eggwhite lysozyme as a model protein. The molecular identification of lysine and arginine modification sites was provided by molecular weight determinations of modified and unmodified tryptic peptide mixtu...

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Selective chemical modification of DNA with alkoxy- and benzyloxyamines.

A new method for the selective chemical modification of DNA at cytosine nucleobases using alkoxy- and benzyloxyamines is presented. It is shown that in particular benzyloxyamines are effective DNA modifying agents, giving rise to almost exclusive formation of the mono addition products. By using a bifunctional derivative, that is, p-azidobenzyloxyamine hydrochloride, an azide moiety, which is a...

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A "tag-and-modify" approach to site-selective protein modification.

Covalent modification can expand a protein's functional capacity. Fluorescent or radioactive labeling, for instance, allows imaging of a protein in real time. Labeling with an affinity probe enables isolation of target proteins and other interacting molecules. At the other end of this functional spectrum, protein structures can be naturally altered by enzymatic action. Protein-protein interacti...

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ژورنال

عنوان ژورنال: Nature Communications

سال: 2014

ISSN: 2041-1723

DOI: 10.1038/ncomms5740