Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM022994-10S1
Application #
3271441
Study Section
(SSS)
Project Start
1985-01-01
Project End
1985-11-30
Budget Start
1985-01-01
Budget End
1985-11-30
Support Year
10
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Colorado State University-Fort Collins
Department
Type
Schools of Arts and Sciences
DUNS #
112617480
City
Fort Collins
State
CO
Country
United States
Zip Code
80523
Liu, Zhigang; Chen, Kang; Ng, Angela et al. (2004) Solvent dependence of PII conformation in model alanine peptides. J Am Chem Soc 126:15141-50
Woody, Robert W (2004) Circular dichroism of protein-folding intermediates. Methods Enzymol 380:242-85
Pescitelli, Gennaro; Gabriel, Sven; Wang, Yuekui et al. (2003) Theoretical analysis of the porphyrin-porphyrin exciton interaction in circular dichroism spectra of dimeric tetraarylporphyrins. J Am Chem Soc 125:7613-28
Sreerama, Narasimha; Woody, Robert W (2003) Structural composition of betaI- and betaII-proteins. Protein Sci 12:384-8
Woody, A-Young Moon; Woody, Robert W (2003) Individual tyrosine side-chain contributions to circular dichroism of ribonuclease. Biopolymers 72:500-13
Kiefl, Christoph; Sreerama, Narasimha; Haddad, Raid et al. (2002) Heme distortions in sperm-whale carbonmonoxy myoglobin: correlations between rotational strengths and heme distortions in MD-generated structures. J Am Chem Soc 124:3385-94
Woody, Robert W; Koslowski, Axel (2002) Recent developments in the electronic spectroscopy of amides and alpha-helical polypeptides. Biophys Chem 101-102:535-51
Chin, Der-Hang; Woody, Robert W; Rohl, Carol A et al. (2002) Circular dichroism spectra of short, fixed-nucleus alanine helices. Proc Natl Acad Sci U S A 99:15416-21
Mou, Tung-Chung; Sreerama, Narasimha; Terwilliger, Thomas C et al. (2002) Independent tyrosyl contributions to the CD of Ff gene 5 protein and the distinctive effects of Y41H and Y41F mutants on protein-protein cooperative interactions. Protein Sci 11:601-13
Kamen, Douglas E; Woody, Robert W (2002) Identification of proline residues responsible for the slow folding kinetics in pectate lyase C by mutagenesis. Biochemistry 41:4724-32

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