Proteins recognizing

Figure 10.19 Heterodimerization of leucine zipper proteins can alter their DNA-binding specificity. Leucine zipper homodimers bind to symmetric DNA sequences, as shown In the left-hand and center drawings. These two proteins recognize different DNA sequences, as indicated by the red and blue regions in the DNA. The two different monomers can combine to form a heterodimer that recognizes a hybrid DNA sequence, composed of one red and one blue region.

Koga, T., Wand, W.A., DeBruyn, J., Munk, M.E., Schoel, B., Kaufmann, S.H. (1989). T cells against a bacterial heat shock protein recognize stressed macrophages. Science 245, 1112—1115. 

The repressOT protein recognized only free acids inducers. However, as already observed, the in vivo tests can be realized with the corresponding esters, since they are hydrolysed in situ by esterases. 

Hoey, T. H., and Levine, M. (1988). Divergent homeobox proteins recognize similar DNA sequences in Drosophila. Nature 332 858-861. 

Tc-SOD-1) has been cloned and expressed (Matzilevich et al., 1999, unpublished results). While antibodies to this protein recognize a dimer of 20/22 kDa in larval extracts, evidence has yet to be obtained that this gene product is represented in larval TES. In addition, several more SOD genes have been identified by an EST project from a cDNA library from this stage. It seems likely, but has yet to be demonstrated, that SODs represent an important part of the parasite s defence mechanism against immune attack, as has been shown for other nematodes (James, 1994 Ou et al, 1995). 

Major groove binders. Mainly proteins recognize the major... 

Figure 12. Generalized scheme for the formation of a polymeric network with imprinted cavities base d on the chemical and special characteristics of the template (T) the natural polymerlike antibody-type proteins recognize xenobiotics, a fully synthetic polymer may recognize the preentrapped and afterwards washed out template (T) molecule.

The complexity of regulation of Raf kinase was shown by the discovery of a further three proteins which can specifically associate with Raf kinase (review Morrison and Cutler, 1997, Sternberg and Alberola-Ila, 1998). Members of the family of 14-3-3 proteins are found associated with Raf kinase. The 14-3-3 proteins recognize and bind phosphoserine residues in a particular sequence environment. It is assumed that the 14-3-3 proteins bind to Ser-phosphate residues of Raf kinase and thereby fix it in an inactive conformation. Other Raf-interacting proteins include the molecular chaperones hsp90 and p50. These proteins appear to be important for maintaining protein stability and for the proper localization of Raf kinase within the cell. 

Old yellow enzyme , first protein recognized Warburg and Christian 4)... 

Interaction between DNA and DNA-Binding Proteins Recognizing Specific Regions in the DNA Duplex The Helix-Turn-Helix Is the Most Common Motif Found in Prokaryotic Regulatory Proteins Helix-Turn-Helix Regulatory Proteins Are Symmetrical... 

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