Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM021479-18S1
Application #
3270536
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1977-12-01
Project End
1995-06-30
Budget Start
1993-04-01
Budget End
1993-06-30
Support Year
18
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Oregon State University
Department
Type
Schools of Arts and Sciences
DUNS #
053599908
City
Corvallis
State
OR
Country
United States
Zip Code
97339
Macdonald, J R; Johnson Jr, W C (2001) Environmental features are important in determining protein secondary structure. Protein Sci 10:1172-7
Krittanai, C; Johnson Jr, W C (2000) The relative order of helical propensity of amino acids changes with solvent environment. Proteins 39:132-41
King, S M; Johnson, W C (1999) Assigning secondary structure from protein coordinate data. Proteins 35:313-20
Johnson, W C (1999) Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35:307-12
Krittanai, C; Johnson, W C (1997) Correcting the circular dichroism spectra of peptides for contributions of absorbing side chains. Anal Biochem 253:57-64
Johnson Jr, W C; Palczewski, K; Gorczyca, W A et al. (1997) Calcium binding to recoverin: implications for secondary structure and membrane association. Biochim Biophys Acta 1342:164-74
Zhong, L; Putnam, R J; Johnson Jr, W C et al. (1995) Design and synthesis of amphipathic antimicrobial peptides. Int J Pept Protein Res 45:337-47
Hirschberg, B T; Mosser, V A; Peterson, G L et al. (1995) Kinetic and biophysical analysis of the m2 muscarinic receptor. Life Sci 56:907-13
Peterson, G L; Toumadje, A; Johnson Jr, W C et al. (1995) Purification of recombinant porcine m2 muscarinic acetylcholine receptor from Chinese hamster ovary cells. Circular dichroism spectra and ligand binding properties. J Biol Chem 270:17808-14
Bloemendal, M; Johnson Jr, W C (1995) Structural information on proteins from circular dichroism spectroscopy possibilities and limitations. Pharm Biotechnol 7:65-100

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