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References:

  1. Wong TS, Roccatano D, Zacharias M, Schwaneberg U. A statistical analysis of random mutagenesis methods used for directed protein evolution. J Mol Biol 2006, 355(4):858-871. Link

  2. Wong TS, Zhurina D, Schwaneberg U. The diversity challenge in directed protein evolution. Comb Chem High Throughput Screen 2006, 9(4):271-288. Link

  3. Wong TS, Roccatano D and Schwaneberg U. Are transversion mutations better? A MAP-analysis on P450 BM-3 heme domain. Biotechnol J. 2007, 2:133-142. Link

  4. Wong TS, Roccatano D, Schwaneberg U. Steering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries. Environ Microbiol 2007, 9(11):2645-2659. Link

  5. Wong TS, Roccatano D and Schwaneberg U. Challenges of the genetic code for exploring sequence space in directed protein evolution. Biocatal Biotransfor 2007. 25: 229-241. Link

  6. Jmol: an open-source Java viewer for chemical structures in 3D. Link

  7. Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22(12):2577-2637. Link

  8. Chothia C. The nature of the accessible and buried surfaces in proteins. J Mol Biol 1976, 105: 1-12. Link

  9. Kumar S, Nussinov R. Close-range electrostatic interactions in proteins. Chembiochem 2002, 3(7):604-617. Link

  10. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157(1):105-132. Link

  11. Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 1985, 229(4708):23-28. Link

  12. Overington J, Johnson MS, Sali A, Blundell TL. Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc Biol Sci 1990, 241(1301):132-145. Link

Reference: Verma R, Schwaneberg U, Roccatano D 2012. MAP2.03D: A sequence/structure based server for protein engineering  
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