The recent availability of X-ray structures and new biophysical measurements have shed further light on the detailed mechanism of carbonic anhydrase and its inhibition. It is noted that in some instances the structural information obtained through X-ray analysis of single crystals and NMR measurements in solution disagree. We take these conflicting results as possible conformations close in energies, both of which can be used to design the enzymatic pathway.

Carbonic anhydrase: an example of how the cavity governs the reactivity at the zinc ion / I.Bertini; C.Luchinat; S.Mangani; R.Pierattelli. - In: COMMENTS ON INORGANIC CHEMISTRY. - ISSN 0260-3594. - STAMPA. - 17:(1995), pp. 1-15.

Carbonic anhydrase: an example of how the cavity governs the reactivity at the zinc ion

BERTINI, IVANO;LUCHINAT, CLAUDIO;PIERATTELLI, ROBERTA
1995

Abstract

The recent availability of X-ray structures and new biophysical measurements have shed further light on the detailed mechanism of carbonic anhydrase and its inhibition. It is noted that in some instances the structural information obtained through X-ray analysis of single crystals and NMR measurements in solution disagree. We take these conflicting results as possible conformations close in energies, both of which can be used to design the enzymatic pathway.
1995
17
1
15
I.Bertini; C.Luchinat; S.Mangani; R.Pierattelli
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/352341
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