Ways and means of coping with uncertainties of the relationship of the genetic blue print to protein structure and function in the cell

Abstract

As one of the disciplines of systems biology, proteomics is central to enabling the elucidation of protein function within the cell; furthermore, the question of how to deduce protein structure and function from the genetic readout has gained new significance. This problem is of particular relevance for proteins engaged in cell signalling. In dealing with this question, I shall critically comment on the reliability and predictability of transmission and translation of the genetic blue print into the phenotype, the protein. Based on this information, I will then evaluate the intentions and goals of today's proteomics and gene-networking and appraise their chances of success. Some of the themes commented on in this publication are explored in greater detail with particular emphasis on the historical roots of concepts and techniques in my forthcoming book, published in German: Von Molekülen zu Zellen. 100 Jahre experimentelle Biologie. Betrachtungen eines Biochemikers.

Advance of signal transduction pathways in normal cell

“…We will not introduce this kind of pathway particularly. can bind GTP or GDP, and activate GTPase which could bound GTP to form GDP, and their conformational changes can then activate efecter proteins, thus transport the extracellular signal into the cell (Helmreich EJ, 2010). On the basis of based on the efects to correlated enzymes produced by G proteins, they are divided into stimulatory G proteins (Gs) and inhibitory G proteins (Gi).…”

“…G protein (GTP binding protein) or guanine nucleotide‐ binding regulatory protein, has a 7 transmembrane α‐helix structure with N ending of membrane and C ending in the cell, and can bind with guanosine triphosphate (GTP) or guanosine triphosphate (GDP) (Hilf G et al, 1992). All the members in this family have the same characters that are consisted of three different subunits‐α, β, γ and can bind GTP or GDP, and activate GTPase which could bound GTP to form GDP, and their conformational changes can then activate effecter proteins, thus transport the extracellular signal into the cell (Helmreich EJ, 2010). On the basis of based on the effects to correlated enzymes produced by G proteins, they are divided into stimulatory G proteins (Gs) and inhibitory G proteins (Gi).…”

“…However, this kind of receptors enzyme can activate themselves and their structure is mono‐transmembrane. When the receptors are activated, they can exert function as enzymes (Helmreich EJ, 2010). There are four types of these receptors including guanylate cyclase receptors catalyzing the production of cGMP in the cytoplasm, tyrosine tyrosine‐protein kinase receptors phosphorating specific tyrosine residues of some signal transduction proteins in the cytoplasm, tyrosine phosphatase receptors removing a phosphate group from the signal transduction proteins and Ser/Thr protein kinase receptors phosphorating Ser/Thr residues of some signal transduction proteins in the cytoplasm (Schulz S et al, 1989).…”