Download e-book for kindle: A Random Walk in Science, by Robert L. Weber

By Robert L. Weber

ISBN-10: 085498027X

ISBN-13: 9780854980277

This anthology offers an perception into the wit and mind of the medical brain via a mix of a laugh and critical contributions written by means of and approximately scientists. The contributions checklist altering attitudes inside of technological know-how and replicate the interactions of technology with society.

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37. Morales TI, Hascall VC. Effects of interleu~n-land lipopolysaccharides on protein and carbohydratemetabolism in bovine articularcartilage organ cultures. Connective Tiss Res 1989; 19:255-275. 38. Grebner EE, Wall CW, Neufeld EF. Glycosylation of serine residues by a uridine diphosphate-xy1ose:proteinxylosyltransferase from mouse mastocytoma. Arch Biochem Biophys 1966; 116391-398, 39. Robinson HC, Telser A, Dorfrnan A. Studies on the biosynthesis of the linkage region of chondroitin-sulfateprotein complex.

In contrast a recent x-ray analysis of cocrystals of a heparin decasaccharide and aFGF revealed what was claimed to be biologically active dimers in a “trans” orientation (47) (Fig. 4b). These dimers lacked a protein-protein interface and the receptor-binding regions were directed away from the saccharide chain. It will be important to determine whether the dimer symmetry in these models is compatible with high-affinity binding and dimerization of the FGFRs. , binding of one bFGF molecule to HS would increase the probability of binding a second one in close proximity) but there is no evidence for this (29).

I Z ~ 1. Reco~nitionProperties Acidic and basic FCF (aFGFIFGF-1 and bFGFIFGF-2, respectively) are the prototypic members of the FCF family and they both depend on HS for optimum cell signaling and stimulation of cell growth (26). They are quite small (approximately 18 kDa), compact, monomeric proteins and their highly homologous HS binding regions are formed by a composite of discontinuous surface loops that extend from a core of centrally positioned p strands (2’7,28). The HS binding site of bFGF accommodates five sugar residues, including a key IdoA,2S residue (29), and a minimal binding sequence of GlcNS03a1 -4 IdoA(2S) a 1 4 GlcNS03al4 IdoA a 1 -4 ClcNS03 can be deduced from x-ray analysis of cocrystals of heparin saccharides and bFGF (30).

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A Random Walk in Science, by Robert L. Weber

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