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1.
Chem Commun (Camb) ; 53(80): 11036-11039, 2017 Oct 05.
Article in English | MEDLINE | ID: mdl-28937163

ABSTRACT

The effect of charged versus neutral N- and C-termini on the stability of the collagen triple helix was examined. Thermal denaturation studies at different pH with collagen model peptides showed that an ammonium group at the N-terminus destabilizes the triple helix more than a carboxylate at the C-terminus. A neutral carboxylic acid stabilizes the triple helix more than an amido moiety at the C-terminus.


Subject(s)
Collagen/chemistry , Carboxylic Acids/chemistry , Hydrogen-Ion Concentration , Protein Denaturation , Protein Stability , Protein Structure, Secondary , Temperature
2.
Org Biomol Chem ; 14(24): 5529-33, 2016 Jun 28.
Article in English | MEDLINE | ID: mdl-26876694

ABSTRACT

We use kinetic data, photophysical properties, and mechanistic analyses to compare recently developed high-rate constant oxime and hydrazone formations. We show that when Schiff base formation between aldehydes and arylhydrazines is carried out with an appropriately positioned boron atom, then aromatic B-N heterocycles form irreversibly. These consist of an extended aromatic structure amenable to the tailoring of specific properties such as reaction rate and fluorescence. The reactions work best in neutral aqueous buffer and can be designed to be fluorogenic - properties which are particularly interesting in bioconjugation.

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