Enzyme activity and flexibility at very low hydration.

Abstract:

:Recent measurements have demonstrated enzyme activity at hydrations as low as 3%. This raises the question of whether hydration-induced enzyme flexibility is important for activity. Here, to address this, picosecond dynamic neutron scattering experiments are performed on pig liver esterase powders at 0%, 3%, 12%, and 50% hydration by weight and at temperatures ranging from 120 to 300 K. At all temperatures and hydrations, significant quasielastic scattering intensity is found in the protein, indicating the presence of anharmonic, diffusive motion. As the hydration increases, a temperature-dependent dynamical transition appears and strengthens involving additional diffusive motion. The implication of these results is that, although the additional hydration-induced diffusive motion in the protein detected here may be related to increased activity, it is not required for the enzyme to function.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Kurkal V,Daniel RM,Finney JL,Tehei M,Dunn RV,Smith JC

doi

10.1529/biophysj.104.058677

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

1282-7

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(05)72775-2

journal_volume

89

pub_type

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