An ESEEM investigation of Cu(II)-Insulin in polycrystalline samples has revealed that the quadrupole parameters for the remote nitrogen of the two equatorial HIS imidazoles bound to copper are similar to those found in type I copper proteins. When Cd(II) ions are allowed to soak into these crystalline samples a dramatic switch is observed in these parameters, which change to values more similar to those found in type II copper sites. FT-ESEEM simulations based on atomic positions derived from Insulin crystal structures show that this switch is due to a change in the hydrogen bonding environment of the remote nitrogen.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002583-13
Application #
6281730
Study Section
Project Start
1998-05-05
Project End
2000-04-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
13
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461
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