Electrostatic properties of alpha/beta-barrel enzymes were studied by examining the structures of six enzymes containing this fold: triose phosphate isomerase, fructose-1,6-biophosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase and of narbonin, a protein with this fold but without any known enzymatic activity. The backbone of the alpha/beta-barrel has a distinct electrostatic field pattern, which contributes substantially to the enzyme's (protein) overall electrostatic fingerprints. When the side-chains are included in the calculations, the electrostatic pattern observed for the backbone is globally conserved and the number of electric field lines per unit surface increases. The electrostatic field calculated in this work are consistent with the known preference of this family of enzymes for negatively charged substrates. The calculations were carried out using the program DelPhi.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR004293-09
Application #
6309534
Study Section
Project Start
1999-12-01
Project End
2000-11-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
9
Fiscal Year
2000
Total Cost
$24,318
Indirect Cost
Name
Cornell University
Department
Type
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
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