Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM046870-05
Application #
2184360
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1992-08-01
Project End
1999-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
5
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of California Santa Cruz
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Santa Cruz
State
CA
Country
United States
Zip Code
95064
Aronoff-Spencer, E; Burns, C S; Avdievich, N I et al. (2000) Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry 39:13760-71
Monaco, V; Formaggio, F; Crisma, M et al. (1999) Orientation and immersion depth of a helical lipopeptaibol in membranes using TOAC as an ESR probe. Biopolymers 50:239-53
Bennati, M; Gerfen, G J; Martinez, G V et al. (1999) Nitroxide side-chain dynamics in a spin-labeled helix-forming peptide revealed by high-frequency (139.5-GHz) EPR spectroscopy. J Magn Reson 139:281-6
Bolin, K A; Anderson, D J; Trulson, J A et al. (1999) NMR structure of a minimized human agouti related protein prepared by total chemical synthesis. FEBS Lett 451:125-31
Trulson, J A; Millhauser, G L (1999) The effect of mutations on peptide models of the DNA binding helix of p53: evidence for a correlation between structure and tumorigenesis. Biopolymers 49:215-24
Martinez, G V; Millhauser, G L (1998) A neural network approach to the rapid computation of rotational correlation times from slow motional ESR spectra. J Magn Reson 134:124-30
Lundberg, K M; Stenland, C J; Cohen, F E et al. (1997) Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR. Chem Biol 4:345-55
Severcan, F; Stenland, C; Millhauser, G (1997) ESR studies of pig citrate synthase. Biochem Soc Trans 25:380S
Millhauser, G L; Stenland, C J; Hanson, P et al. (1997) Estimating the relative populations of 3(10)-helix and alpha-helix in Ala-rich peptides: a hydrogen exchange and high field NMR study. J Mol Biol 267:963-74
Millhauser, G L; Stenland, C J; Bolin, K A et al. (1996) Local helix content in an alanine-rich peptide as determined by the complete set of 3JHN alpha coupling constants. J Biomol NMR 7:331-4

Showing the most recent 10 out of 17 publications