Biochemistry of Signal Transduction and Regulation by Gerhard Krauss

By Gerhard Krauss

This all-new variation of a best-selling textual content has been completely up to date to maintain velocity with the fast development in sign transduction research.
With didactic ability and readability, the molecular foundation of sign transduction, regulated gene expression, the cellphone cycle, tumorigenesis and apoptosis is made obvious for everybody with a easy wisdom in biochemistry or molecular biology.
"Valuable up to date info on biochemistry of sign transduction and regulation" (AFS)
"The transparent and didactic presentation makes it a textbook very necessary for college kids and researchers no longer acquainted with all elements of phone regulation." (Biochemistry)
"This ebook is de facto books: legislation and sign Transduction." (Drug Research)

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15. Bending of the DNA in the CAP protein-DNA complex. The CAP protein (E. coli) binds as a dimer to the two-fold symmetric operator sequence. The DNA is bent nearly 90deg in the complex. The turns are centered around two GT sequences (shown in black) of the recognition element. 20 1 The Regulation of Gene Expression Fig. 16. Bending of DNA in the TATA box. , 1993). The DNA is deformed in the region near the kink: the minor groove, which faces the protein, is clearly widened. Molscript drawing (Kraulis, 1991).

It is therefore assumed that two dimers of the repressor associate to form the active tetramer, whereby one of the two dimers is bound to O3, the other dimer binds to O1. The intervening DNA forms a so-called repression loop. , 1996. 24 1 The Regulation of Gene Expression The distance and nature of the bases between both the palindromic as well as the direct repeats of the recognition sequence plays an important role. It is evident that a dimeric protein would bind optimally to a 2-fold symmetric sequence only if the distance between the recognition elements matches the distance as determined by the protein structure.

The ionic interactions are, however, less suitable to distinguish between various base pairs since only the phosphates of the backbone from the DNA are involved in the interaction. Together with the specific H-bonds, the non-specific ionic interactions contribute significantly to the formation of a stable complex. The positively charged surface of DNA-binding proteins is also the reason for the ability of many such proteins to bind DNA nonspecifically. The compensation of the negative charges of DNA can also have a further effect.

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