The basic aim of this research is to determine the conformation of natural nucleic acids and their synthetic counterparts using circular dichroism (CD) spectroscopy and related techniques. CD is an excellent technique for monitoring the secondary structure of optically active biological molecules, since it is very sensitive to the orientation of nearest neighbor chromophores, and since it can be used when these molecules are in solution. The conformation of biological molecules helps determine reactions which they undergo, and thus we expect to learn about the relationships between the conformation of the various nucleic acids and their biological function. However, CD is a relatively new technique and a great deal of basic work remains to be done if one is to relate a CD spectrum directly to the secondary structure of the biological molecule. At the same time that we are investigating the conformation of nucleic acids, we are also trying to improve the technique both experimentally and theoretically so that it will be more useful.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM021479-11
Application #
3270537
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1977-12-01
Project End
1985-11-30
Budget Start
1984-12-01
Budget End
1985-11-30
Support Year
11
Fiscal Year
1985
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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