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Functions binding properties

The 434 Cro molecule contains 71 amino acid residues that show 48% sequence identity to the 69 residues that form the N-terminal DNA-binding domain of 434 repressor. It is not surprising, therefore, that their three-dimensional structures are very similar (Figure 8.11). The main difference lies in two extra amino acids at the N-terminus of the Cro molecule. These are not involved in the function of Cro. By choosing the 434 Cro and repressor molecules for his studies, Harrison eliminated the possibility that any gross structural difference of these two molecules can account for their different DNA-binding properties. [Pg.137]

The polypeptide chain of p53 is divided in three domains, each with its own function (Figure 9.16). Like many other transcription factors, p53 has an N-terminal activation domain followed by a DNA-binding domain, while the C-terminal 100 residues form an oligomerization domain involved in the formation of the p53 tetramers. Mutants lacking the C-terminal domain do not form tetramers, but the monomeric mutant molecules retain their sequence-specific DNA-binding properties in vitro. [Pg.167]

Some by-products from the food industry contain high proportions of plant cell walls which can be used in human nutrition to produce "dietary fibre" or "functional fibre", i.e. compounds which can be used for their water-holding/binding properties, oil-binding capacity,... or as a source of polysaccharides such as pectins which are suitable after extraction, as gelling or thickening agents. [Pg.425]

Kontopidis, G., Holt, C., and Sawyer, L. (2004). Invited review Beta-lactoglobulin Binding properties, structure, and function. /. Dairy Sci. 87, 785-796. [Pg.197]

Absorption and Raman analysis of LHCII complexes from xanthophyll biosynthesis mutants and plants containing unusual carotenoids (e.g., lactucoxanthin and lutein-epoxide) should also be interesting, since the role of these pigments and their binding properties are unknown. Understanding the specificity of binding can help to understand the reasons for xanthophyll variety in photosynthetic antennae and aid in the discovery of yet unknown functions for these molecules. [Pg.133]

In an attempt to prepare a catalytically active cycloamylose derivative which would retain the binding properties of an unmodified cycloamylose,7 Gruhn and Bender (1971) attached a relatively small hydroxamate function to a secondary hydroxyl group of cyclohexaamylose. The initial and most important step in the synthetic sequence is the reaction of ionized cyclo-... [Pg.253]

E. K. Woller and M. J. Cloninger, The lectin-binding properties of six generations of mannose-functionalized dendrimers, Org. Lett., 4 (2002) 7-10. [Pg.389]

These families are defined by individual members, which are related to each other by common primary sequences, structural motifs and binding properties (e.g. Fig. 7-1). In spite of differences in the biochemistry and function of each CAM, we can make certain generalizations about how they function in nervous tissue. First, CAMs act at... [Pg.111]

Ras and its relatives are subjects of intensive investigations by biological, biochemical, biophysical, and medical studies. Within just one decade more than 17,000 articles (Medline, 1966-2000) deal with function and properties of this protein. Structural and functional data, based on Ras as a prototype, have provided insight into the basic principles of GTP-binding proteins, their activation, de-activation, and signal transmission. [Pg.108]

Also on the nucleic acid field, it has been shown95 that the distribution pattern of NH2/NH3 + /OH groups in natural aminoglycosides could indirectly influence their RNA binding properties and therefore their antibiotic functions. Indeed, the number and location of these polar groups is essential to modulate the conformation and dynamics of the glycoside with the concomitant implication for the RNA recognition process. [Pg.346]

Briggs, M., Gierasch, L., Zlotnick, A., Lear,J., and DeGrado, W. (1985). In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides. Science 228, 1096—1099. [Pg.332]


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