http://www.bmb.colostate.edu Department of Biochemistry and Molecular Biology - College of Natural Sciences - Colorado State University Mon, 06 May 2013 20:11:58 +0000 en-US hourly 1 http://wordpress.org/?v=3.5 http://www.bmb.colostate.edu/publications/the-exciton-model-and-the-circular-dichroism-of-polypeptides/?utm_source=rss&utm_medium=rss&utm_campaign=the-exciton-model-and-the-circular-dichroism-of-polypeptides http://www.bmb.colostate.edu/publications/the-exciton-model-and-the-circular-dichroism-of-polypeptides/#comments Tue, 21 Feb 2012 17:54:57 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1386 R. W. Woody, Monatsh, “The exciton model and the circular dichroism of polypeptides”, Chem. 136, 347-366 (2005).

]]> http://www.bmb.colostate.edu/publications/the-exciton-model-and-the-circular-dichroism-of-polypeptides/feed/ 0 http://www.bmb.colostate.edu/publications/single-peptide-bonds-exhibit-polyproii-random-coil-circular-dichroism-spectra/?utm_source=rss&utm_medium=rss&utm_campaign=single-peptide-bonds-exhibit-polyproii-random-coil-circular-dichroism-spectra http://www.bmb.colostate.edu/publications/single-peptide-bonds-exhibit-polyproii-random-coil-circular-dichroism-spectra/#comments Tue, 21 Feb 2012 17:54:42 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1384 I. Gokce, R. W. Woody, G. Anderluh, and J. H. Lakey, “Single peptide bonds exhibit poly(Pro)II (random coil) circular dichroism spectra”, J. Am. Chem. Soc. 127, 9700-9701 (2005).

]]> http://www.bmb.colostate.edu/publications/single-peptide-bonds-exhibit-polyproii-random-coil-circular-dichroism-spectra/feed/ 0 http://www.bmb.colostate.edu/publications/heme-heme-interactions-in-tetramers-and-dimers-of-hemoglobin-subunits-devoe-theory-calculations/?utm_source=rss&utm_medium=rss&utm_campaign=heme-heme-interactions-in-tetramers-and-dimers-of-hemoglobin-subunits-devoe-theory-calculations http://www.bmb.colostate.edu/publications/heme-heme-interactions-in-tetramers-and-dimers-of-hemoglobin-subunits-devoe-theory-calculations/#comments Tue, 21 Feb 2012 17:54:28 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1382 R. W. Woody, “Heme-heme interactions in tetramers and dimers of hemoglobin subunits — DeVoe theory calculations”, Chirality 17, 450-455 (2005).

]]> http://www.bmb.colostate.edu/publications/heme-heme-interactions-in-tetramers-and-dimers-of-hemoglobin-subunits-devoe-theory-calculations/feed/ 0 http://www.bmb.colostate.edu/publications/intrinsic-protein-disorder-amino-acid-composition-and-the-histone-terminal-domains/?utm_source=rss&utm_medium=rss&utm_campaign=intrinsic-protein-disorder-amino-acid-composition-and-the-histone-terminal-domains http://www.bmb.colostate.edu/publications/intrinsic-protein-disorder-amino-acid-composition-and-the-histone-terminal-domains/#comments Tue, 21 Feb 2012 17:54:09 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1380 J. C. Hansen, X. Lu, E. D. Ross, and R. W. Woody, “Intrinsic protein disorder, amino acid composition, and the histone terminal domains”, J. Biol. Chem. 281, 1853-1857 (2006).

]]> http://www.bmb.colostate.edu/publications/intrinsic-protein-disorder-amino-acid-composition-and-the-histone-terminal-domains/feed/ 0 http://www.bmb.colostate.edu/publications/theoretical-investigation-of-the-photo-initiated-folding-of-hp-36/?utm_source=rss&utm_medium=rss&utm_campaign=theoretical-investigation-of-the-photo-initiated-folding-of-hp-36 http://www.bmb.colostate.edu/publications/theoretical-investigation-of-the-photo-initiated-folding-of-hp-36/#comments Tue, 21 Feb 2012 17:53:56 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1378 S. Jang, N. Sreerama, V. H.-C. Liao, S.-F. Lu, F.-Y. Li, S. Shin, R. W. Woody, and S.-H. Lin, “Theoretical investigation of the photo-initiated folding of HP-36″, Protein Sci. 15, 2290-2299 (2006).

]]> http://www.bmb.colostate.edu/publications/theoretical-investigation-of-the-photo-initiated-folding-of-hp-36/feed/ 0 http://www.bmb.colostate.edu/publications/conformational-changes-upon-calcium-binding-and-phosphorylation-in-a-synthetic-fragment-of-calmodulin/?utm_source=rss&utm_medium=rss&utm_campaign=conformational-changes-upon-calcium-binding-and-phosphorylation-in-a-synthetic-fragment-of-calmodulin http://www.bmb.colostate.edu/publications/conformational-changes-upon-calcium-binding-and-phosphorylation-in-a-synthetic-fragment-of-calmodulin/#comments Tue, 21 Feb 2012 17:53:43 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1376 L. Settimo, S. Donnini, A. H. Juffer, R. W. Woody, and O. Mariano, “Conformational changes upon calcium binding and phosphorylation in a synthetic fragment of calmodulin”, Pept. Sci. 88, 373-385 (2007).

]]> http://www.bmb.colostate.edu/publications/conformational-changes-upon-calcium-binding-and-phosphorylation-in-a-synthetic-fragment-of-calmodulin/feed/ 0 http://www.bmb.colostate.edu/publications/gauging-a-hydrocarbon-ruler-by-an-intrinsic-exciton-probe/?utm_source=rss&utm_medium=rss&utm_campaign=gauging-a-hydrocarbon-ruler-by-an-intrinsic-exciton-probe http://www.bmb.colostate.edu/publications/gauging-a-hydrocarbon-ruler-by-an-intrinsic-exciton-probe/#comments Tue, 21 Feb 2012 17:53:29 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1374 M. A. Khan, C. Neale, C. Michaux, R. Pomés, G. G. Privé, R. W. Woody, and R. E. Bishop, “Gauging a hydrocarbon ruler by an intrinsic exciton probe”, Biochemistry 46, 4565-4579 (2007).

]]> http://www.bmb.colostate.edu/publications/gauging-a-hydrocarbon-ruler-by-an-intrinsic-exciton-probe/feed/ 0 http://www.bmb.colostate.edu/publications/aromatic-side-chain-contributions-to-protein-circular-dichroism/?utm_source=rss&utm_medium=rss&utm_campaign=aromatic-side-chain-contributions-to-protein-circular-dichroism http://www.bmb.colostate.edu/publications/aromatic-side-chain-contributions-to-protein-circular-dichroism/#comments Tue, 21 Feb 2012 17:53:14 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1372 R. W. Woody, “Aromatic side-chain contributions to protein circular dichroism”, in Methods in Protein Structure and Stability Analysis: Luminescence Spectroscopy and Circular Dichroism, V. N. Uversky and E. A. Permyakov, eds., Nova Science Publishers, New York, pp. 291-344 (2007).

]]> http://www.bmb.colostate.edu/publications/aromatic-side-chain-contributions-to-protein-circular-dichroism/feed/ 0 http://www.bmb.colostate.edu/publications/inherent-chirality-dominates-the-visiblenear-ultraviolet-cd-spectrum-of-rhodopsin/?utm_source=rss&utm_medium=rss&utm_campaign=inherent-chirality-dominates-the-visiblenear-ultraviolet-cd-spectrum-of-rhodopsin http://www.bmb.colostate.edu/publications/inherent-chirality-dominates-the-visiblenear-ultraviolet-cd-spectrum-of-rhodopsin/#comments Tue, 21 Feb 2012 17:52:59 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1370 G. Pescitelli, N. Sreerama, P. Salvadori, K. Nakanishi, N. Berova, and R. W. Woody, “Inherent chirality dominates the visible/near-ultraviolet CD spectrum of rhodopsin”, J. Am. Chem. Soc., 130, 6170-6181 (2008).

]]> http://www.bmb.colostate.edu/publications/inherent-chirality-dominates-the-visiblenear-ultraviolet-cd-spectrum-of-rhodopsin/feed/ 0 http://www.bmb.colostate.edu/publications/the-circular-dichroism-spectrum-of-peptides-in-the-polyproii-conformation/?utm_source=rss&utm_medium=rss&utm_campaign=the-circular-dichroism-spectrum-of-peptides-in-the-polyproii-conformation http://www.bmb.colostate.edu/publications/the-circular-dichroism-spectrum-of-peptides-in-the-polyproii-conformation/#comments Tue, 21 Feb 2012 17:52:41 +0000 Robert Woody http://bmb.wolpe.natsci.colostate.edu/?post_type=publications&p=1368 R. W. Woody, The circular dichroism spectrum of peptides in the poly(Pro)II conformation, J. Am. Chem. Soc. 131, 8234-8245 (2009).

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