Proteins designer

Aqvist J, C Medina and J-E Samuelsson 1994. A New Method for Predicting Binding Affinity Computer-aided Drug Design. Protein Engineering 7 385-391. 

B and W J Howe 1991. Computer Design of Bioactive Molecules - A Method for Receptor-Based Novo Ligand Design. Proteins Structure, Function and Genetics 11 314-328. i H L 1965. The Generation of a Unique Machine Description for Chemical Structures - A hnique Developed at Chemical Abstracts Service. Journal of Chemical Documentation 5 107-113. J 1995. Computer-aided Estimation of Symthetic Accessibility. PhD thesis. University of Leeds, itan R, N Bauman, J S Dixon and R Venkataraghavan 1987. Topological Torsion A New )lecular Descriptor for SAR Applications. Comparison with Other Descriptors. Journal of emical Information and Computer Science 27 82-85. 

G Baumann, C Frdmmel, C Sander. Polarity as a criterion m protein design. Protein Eng 2 239-334, 1989. 

J Aqvist, C Medina, J-E Samuelsson. A new method for predicting binding affinity in computer-aided drag design. Protein Eng 7 385-391, 1994. 

Table 17.3 Amino acid sequences of domain Bl, the designed protein Janus, and Rop...

A gene encoding this sequence was synthesized and the corresponding protein, called Janus, was expressed, purified, and characterized. The atomic structure of this protein has not been determined at the time of writing but circular dichroic and NMR spectra show very clear differences from B1 and equally clear similarities to Rop. The protein is a dimer in solution like Rop and thermodynamic data indicate that it is a stably folded protein and not a molten globule fold like several other designed proteins. 

Gunasekaran K, Ramakrishnan C, Balaram P (1997) Beta-hairpins in proteins revisited lessons for de novo design. Protein Eng 10 1131-1141... 

Liang SD, Grishin NV. Effective scoring function for protein sequence design. Proteins 2004 54 271-81. 

Food Product Design Protein Possibilities. Lynn A. Kuntz, October 1997, http //www.foodproductdesign.eom/archive/1997/1097AP.html... 

Protein molecular organization on solid matrices has intensively been explored in various manners. Although most of these researchers have not paid attention on retainment of protein functions, this chapter focuses on artificially designed protein organizates which are capable of molecular recognition and molecular information transduction. 

Fig. 5. The aromatic cluster of the hydrophobic core of GTD-43, a helrx-loop-helrx dimer, and some of the assigned long-range NOEs that demonstrate the interactions of the aromatic side chains in the folded motif The formation of aromatic clusters has been observed in several designed proteins. Reproduced with permission from J Am Chem Soc (1997) 119 8598. ( 1997 ACS)...

Traditionally, the structural characterization of designed proteins is carried out by CD spectroscopy, which unfortunately provides only limited structural information at the atomic level. As the understanding of protein design develops more proteins appear that have well-defined structures and the determination of their solution structures by NMR spectroscopy is clearly the main tool for elucidating structure-function relationships. Key information is obtained simply from the ID spectrum (Fig. 7). 

Moon, J.B. and Howe, W.J. Computer design ofbioactive molecules a method for receptor-based de novo ligand design. Proteins Struc., Func., Genet. 1991, 11, 314-328. 

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