Proteolysis - Extended Reference List

Expanded References   1. J.C. Kendrew et al., "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis," Nature, 181:662-6, 1958; J.C. Kendrew et al., "Structure of myoglobin," Nature, 185:422-42, 1960. 2. C. Branden, J. Tooze, "Motifs of Protein Structure," Introduction to Protein Structure, Garland Publishing, Inc., New York, pp. 11-30, 1991; J.S. Richardson, "Describing patterns of protein tertiary structure," Methods in Enzymology, 115:341-8, 1985; J.S. Richardson

Deborah Wilkinson
Mar 19, 2000

Expanded References

 

1. J.C. Kendrew et al., "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis," Nature, 181:662-6, 1958; J.C. Kendrew et al., "Structure of myoglobin," Nature, 185:422-42, 1960.

2. C. Branden, J. Tooze, "Motifs of Protein Structure," Introduction to Protein Structure, Garland Publishing, Inc., New York, pp. 11-30, 1991; J.S. Richardson, "Describing patterns of protein tertiary structure," Methods in Enzymology, 115:341-8, 1985; J.S. Richardson, "Schematic drawings of protein structures," Methods in Enzymology, 115:359-80, 1985; J. Janin, C. Chothia, "Domains in proteins: definitions, location, and structural principles," Methods in Enzymology, 115:420-30, 1985.

3. A. Fontana et al., "Limited proteolysis in the study of protein conformation," Proteolytic Enzymes: Tools and Targets, E. Sterchi, W. Stocker (eds.), Springer Verlag, Heidelberg, pp. 253-80, 1999; H. Neurath, "Limited proteolysis, protein folding and physiological regulation," Protein Folding, R. Jaenicke (ed.), ier, New York, pp....

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