Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM030741-05S1
Application #
3278592
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1982-06-01
Project End
1988-05-31
Budget Start
1986-12-15
Budget End
1987-05-31
Support Year
5
Fiscal Year
1987
Total Cost
Indirect Cost
Name
University of Pittsburgh
Department
Type
Schools of Arts and Sciences
DUNS #
053785812
City
Pittsburgh
State
PA
Country
United States
Zip Code
15213
Lanoul, Anatoli; Coleman, Thomas; Asher, Sanford A (2002) UV resonance raman spectroscopic detection of nitrate and nitrite in wastewater treatment processes. Anal Chem 74:1458-61
Asher, S A; Ianoul, A; Mix, G et al. (2001) Dihedral psi angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe. J Am Chem Soc 123:11775-81
Lednev, I K; Karnoup, A S; Sparrow, M C et al. (2001) Transient UV Raman spectroscopy finds no crossing barrier between the peptide alpha-helix and fully random coil conformation. J Am Chem Soc 123:2388-92
Boyden, M N; Asher, S A (2001) UV Raman studies of peptide conformation demonstrate that betanova does not cooperatively unfold. Biochemistry 40:13723-7
Ianoul, A; Boyden, M N; Asher, S A (2001) Dependence of the peptide amide III vibration on the phi dihedral angle. J Am Chem Soc 123:7433-4
Holtz, J S; Lednev, I K; Asher, S A (2000) UV resonance Raman study of angiotensin II conformation in nonaqueous environments: lipid micelles and acetonitrile. Biopolymers 57:55-63
Holtz, J S; Holtz, J H; Chi, Z et al. (1999) Ultraviolet Raman examination of the environmental dependence of bombolitin I and bombolitin III secondary structure. Biophys J 76:3227-34
Chi, Z; Asher, S A (1999) Ultraviolet resonance Raman examination of horse apomyoglobin acid unfolding intermediates. Biochemistry 38:8196-203
Chi, Z; Asher, S A (1998) UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse myoglobin. Biochemistry 37:2865-72
Chi, Z; Chen, X G; Holtz, J S et al. (1998) UV resonance Raman-selective amide vibrational enhancement: quantitative methodology for determining protein secondary structure. Biochemistry 37:2854-64

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