The basic aim of our research is to determine the conformation of biopolymers 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 the reactions which they undergo, and thus we expect to learn about the relationships between the conformation of these molecules and their biological function. At the same time that we are investigating conformation, we are also trying to improve CD, both experimentally and theoretically so that it will be more useful. During the coming year, we will study the secondary structure of proteins of current interest. We will use the methods that we have developed in the past few years for extracting the secondary structures in a protein from its vacuum UV CD spectrum. We will collaborate with appropriate individuals to obtain exciting proteins. We plan to improve our techniques by adding a number of proteins to our basis set and extending the spectra of all proteins to 168 nm. We will also use our methods to investigate the denaturation of simple proteins to determine how the secondary structures come apart on denaturation.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM021479-16
Application #
3270541
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1977-12-01
Project End
1990-11-30
Budget Start
1989-12-01
Budget End
1990-11-30
Support Year
16
Fiscal Year
1990
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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