How the amino acid series of a protein determines its 3-dimensional constitution is an immense challenge in biology and chemistry. best specialists within the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling provide provocative insights into present perspectives at the protein folding challenge and diverse elements for destiny growth.
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Extra info for Ciba Foundation Symposium 161 - Protein Conformation
Rules for the conformations of substituted sidechains. 5-392 Taylor WR 1986 Identification of protein sequence homology by consensus sequence alignment. J Mol Biol 188:233-258 Taylor WR, Orengo CA 1989 Protein structure alignment. J Mol Biol 208:l-22. Comparisons of three-dimensional structure 37 DISCUSSION Holmes: In your refinement procedures do you put in force fields and force constants in the normal way? Blundell: Our probability density tables are really pseudoenergy functions. Andrej Sali has included terms for bonds, bond angles and torsion angles in the form of probability density tables.
Only when both substrates, ATP and AMP, here mimicked by the inhibitor Ap,A, are bound will the arginine residues be fixed in position. We see only the structures I was talking about. Because we find these structures in different crystal packings, meaning that they are in different contact environments, they appear to be the stable structures. Also, we find them in crystals grown from polyethylene glycol and from high ionic strength ammonium sulphate-that is, in quite different solvents. Dodson: I am not questioning that; my question is whether you see an active structure or a potentially active structure in the absence of the substrate in solution-I know you don’t see it in the crystal.
EMBO (Eur Mol Biol Organ) J 9:2351-2359 Ponder JW, Richards FM 1987 Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. 8 A model of xylose isomerase from Actinoplunes rnissouriensis. Proteins Struct Funct Genet 4:165- 172 Schlichting I , Almo SC, Rapp G et a1 1990 Time-resolved X-ray crystallographic study of the confomational change in Ha-Ras p21 protein on GTP hydrolysis. Nature (Lond) 345~309-315 Smith JL, Hendrickson WA, Hontzatko RB, Sherrif S 1986 Structural heterogeneity in protein crystals.