Ciba Foundation Symposium 161 - Protein Conformation

How the amino acid series of a protein determines its three-d constitution is a massive challenge in biology and chemistry. best specialists within the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling supply provocative insights into present perspectives at the protein folding challenge and diverse features for destiny growth.


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Nature (Lond) 345~309-315 Smith JL, Hendrickson WA, Hontzatko RB, Sherrif S 1986 Structural heterogeneity in protein crystals. Biochemistry 25:5018-5027 Smith LJ, Sutcliffe MJ, Redfield C, Dobson CM 1991 Analysis of 6 and X, torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants. Biochemistry 30:986-996 Strynadka N 1990 PhD thesis, University of Alberta, Edmonton, Canada Novartis Foundation Symposium Edited by Derek J. Chadwick, Kate Widdows Copyright 0 1991 by Ciba Foundation Comparative analysis of protein three-dimensional structures and an approach to the inverse folding problem Tom L.

In hexokinase the corresponding structure is altered so that the hydrogen bonds in the 310 helix are not made, with the result that the nucleotide binding site is partly occluded. Rebuilding four residues in hexokinase to form the 310 helix entails moving the adjacent a-helix along by about 2 A. Having done this, one can introduce the ATP coordinates from actin into hexokinase. The y phosphate ends up about 4 A away from the 0 - 6 of the a-toluoyl-glucosamine, which has been bound to hexokinase as a substrate analogue.

Holmes: There’s a wonderful example of that in actin. In hexokinase there is a long helix, 40A long. It’s also present in actin, but there’s a 10-residue insertion in the middle of it. The insertion is a loop that forms part of the actinactin interface in filamentous actin. It does happen, even in Nature! Richards: What does that do t o the registration? Holmes: Nothing. Ptitsyn: I should like to make some comments on the general topology of proteins. The problem, like that Tom Blundell has spoken about, is one of similarity of tertiary folds of different proteins.

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