| Year |
Citation |
Score |
| 1979 |
Ross JBA, Rousslang KW, De Haën C, Lavis VR, Deranleau DA. [12-Homoarginine]glucagon: synthesis and observations on conformation, biological activity, and copper-mediated peptide cleavage Bba - Protein Structure. 576: 372-384. PMID 427194 DOI: 10.1016/0005-2795(79)90412-4 |
0.399 |
|
| 1978 |
Rousslang KW, Ross JBA, Deranleau DA, Kwiram AL. Triplet state of tryptophan in proteins: The nature of the optically detected magnetic resonance lines Biochemistry. 17: 1087-1092. PMID 629948 |
0.585 |
|
| 1978 |
Deranleau DA, Ross JBA, Rousslang KW, Kwiram AL. 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. DOI: 10.1021/Ja00474A043 |
0.613 |
|
| 1978 |
Kwiram AL, Alexander Ross JB, Deranleau DA. Wavelength dependence of the zero-field splittings in the triplet state of tryptophan Chemical Physics Letters. 54: 506-509. DOI: 10.1016/0009-2614(78)85272-5 |
0.578 |
|
| 1977 |
Ross JBA, Rousslang KW, Deranleau DA, Kwiram AL. 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. PMID 200259 DOI: 10.1021/Bi00643A600 |
0.613 |
|
| 1976 |
Teller DC, Deranleau DA. Direct determination of the stoichiometry of charge transfer complexes. Biochimica Et Biophysica Acta. 421: 416-9. PMID 1252475 DOI: 10.1016/0304-4165(76)90309-3 |
0.531 |
|
| 1976 |
Ross JBA, Rousslang KW, Deranleau DA, Kwiram AL. 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. PMID 972232 DOI: 10.1021/Ja00437A089 |
0.599 |
|
| 1976 |
Hinman LM, Coan CR, Deranleau DA. Flexibility in the specificity site of serine proteases. Biochemistry. 15: 2212-9. PMID 945068 DOI: 10.1021/Bi00655A029 |
0.312 |
|
| 1975 |
Coan CR, Hinman LM, Deranleau DA. Charge-transfer studies of the availability of aromatic side chains of proteins in guanidine hydrochloride. Biochemistry. 14: 4421-7. PMID 1174511 DOI: 10.1021/Bi00691A013 |
0.34 |
|
| 1975 |
Deranleau DA, Hinman LM, Coan CR. Effects of pH on the exposure of aromatic donor residues in solution topography studies of bovine trypsin by charge transfer. Journal of Molecular Biology. 94: 567-82. PMID 241855 DOI: 10.1016/0022-2836(75)90322-8 |
0.341 |
|
| 1974 |
Hinman LM, Coan CR, Deranleau DA. Solution topography of proteins by charge transfer. Model complexes, ribonuclease, and lysozyme. Journal of the American Chemical Society. 96: 7067-73. PMID 4436509 DOI: 10.1002/Chin.197502112 |
0.303 |
|
| 1970 |
Radhakrishnan TM, Bradshaw RA, Deranleau DA, Neurath H. The solution conformation of bovine carboxypeptidase a: Reaction with 2-hydroxy-5-nitrobenzyl bromide and N-methylnicotinamide chloride. Febs Letters. 7: 72-76. PMID 11947434 DOI: 10.1016/0014-5793(70)80621-4 |
0.476 |
|
| 1969 |
Deranleau DA, Bradshaw RA, Schwyzer R. The use of n-methylnicotin amide chloride as a conformational probe for chicken egg-white lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 63: 885-9. PMID 4242289 DOI: 10.1073/Pnas.63.3.885 |
0.341 |
|
| 1966 |
Deranleau DA, Neurath H. The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsin Biochemistry. 5: 1413-1425. PMID 5958217 DOI: 10.1021/Bi00868A040 |
0.437 |
|
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