hamon
Online ISSN : 1884-636X
Print ISSN : 1349-046X
ISSN-L : 1349-046X
Neutron Protein Crystallography : Evaluation of pKa of Polar Amino Acid Residues in Proteins
Nobuo Niimura
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2013 Volume 23 Issue 4 Pages 282-287

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Abstract

The biological mechanism of the physiological function such as the enzymatic reaction is well understood by studying protonation states of the catalytic polar amino acid residues, which can be identified by neutron protein crystallography. It is proposed that the protonation states should be systematically discussed from the view point of the pKa values of the amino acid residues in proteins. Several examples of the protonation states of the catalytic residues determined by neutron protein crystallography, such as serine proteases (trypsin, elastase, thrombin, & acromobacter protease I), insulin, hen egg white lysozyme, RNase A, and HIV-1 protease were introduced and discussed on the basis of the pKa values.

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© 2013 The Japanese Society for Neutron Science
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