Kenneth W. Rousslang, PhD

Affiliations: 
1970-1976 Chemistry University of Washington, Seattle, Seattle, WA 
 1976-2009 Chemistry University of Puget Sound, Tacoma, WA, United States 
Area:
Steady-State and Time-Resolved Phosphorescence of biologically important molecules
Google:
"Kenneth Rousslang"
Bio:

Phd, Physical Chemistry University of Washington. Advisor, Alvin Kwirm

Mean distance: 9.07
 
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Publications

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Rousslang KW, Reid PJ, Holloway DM, et al. (2002) Time-resolved phosphorescence of tyrosine, tyrosine analogs, and tyrosyl residues in oxytocin and small peptides. Journal of Protein Chemistry. 21: 547-55
Sato AK, Bitten ER, Senear DF, et al. (1994) Steady-state and time-resolved phosphorescence of wild-type and modified bacteriophage λcI repressors. Journal of Fluorescence. 4: 195-201
Rousslang K, Allen L, Ross JB. (1989) Phosphorescence maxima and triplet state lifetimes of NAD+ and epsilon-NAD+ in ternary complexes with horse liver alcohol dehydrogenase Photochemistry and Photobiology. 49: 137-143
Rousslang KW, Thomasson JM, Ross JBA, et al. (1979) Triplet state of tryptophan in proteins. 2. Differentiation between tryptophan residues 62 and 108 in lysozyme Biochemistry. 18: 2296-2300
Ross JBA, Rousslang KW, De Haën C, et al. (1979) [12-Homoarginine]glucagon: synthesis and observations on conformation, biological activity, and copper-mediated peptide cleavage Bba - Protein Structure. 576: 372-384
Ross JBA, Rousslang KW, Motten AG, et al. (1979) Base interactions in the triplet states of NAD+ and NADH Biochemistry. 18: 1808-1813
Rousslang KW, Ross JBA, Deranleau DA, et al. (1978) Triplet state of tryptophan in proteins: The nature of the optically detected magnetic resonance lines Biochemistry. 17: 1087-1092
Deranleau DA, Ross JBA, Rousslang KW, et al. (1978) Conformations of polypeptide hormones by optically detected magnetic resonance and a Zimm-Bragg analysis of helical folding in glucagon Journal of the American Chemical Society. 100: 1913-1917
Ross JBA, Rousslang KW, Deranleau DA, et al. (1977) Glucagon conformation: Use of optically detected magnetic resonance and phosphorescence of tryptophan to evaluate critical requirements for folding of the polypeptide chain Biochemistry. 16: 5398-5402
Ross JBA, Rousslang KW, Deranleau DA, et al. (1976) Optical detection of magnetic resonance of glucagon and glucagon peptides in solution. A conformational change related to critical length of the peptide chain [46] Journal of the American Chemical Society. 98: 6761-6762
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