NMR studies of fluorophenylalanine-containing carbonic anhydrase.

Abstract:

:Rabbits ingesting 4-fluorophenylalanine are known to incorporate small amounts of this fluorinated amino acid into their proteins. Carbonic anhydrase I isolated from the erythrocytes of animals so maintained exhibits a well-resolved fluorine NMR signal for each phenylalanine in the sequence. The chemical shifts of most of these signals respond to the binding of inhibitors, suggesting that most if not all of the tertiary structure of the enzyme adjusts to the presence of inhibitors at the active site.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gamcsik MP,Gerig JT

doi

10.1016/0014-5793(86)80216-2

subject

Has Abstract

pub_date

1986-02-03 00:00:00

pages

71-4

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80216-2

journal_volume

196

pub_type

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