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Attributs	Valeurs
type	work Issue
Is Part Of	http://hub.abes.fr/oup/periodical/proeng/1994/volume_7
has manifestation of work	http://hub.abes.fr/oup/periodical/proeng/1994/volume_7/issue_5/m/print http://hub.abes.fr/oup/periodical/proeng/1994/volume_7/issue_5/m/web
Date Copyrighted	1994
Rights	© Oxford University Press
issue	5
is Is Part Of of	The prediction and orientation of α-helices from sequence alignments: the combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules Constructing a protein mutant database Intramolecular cavities in globular proteins A pore-forming protein with a metal-actuated switch Three-dimensional structure of a mutant E.coli aspartate aminotransferase with increased enzymic activity A mutational analysis of receptor binding sites of interleukin-1β:differences in binding of human interleukin-1β muteins to human and mouse receptors The use of alanine scanning mutagenesis to determine the role of the N-terminus of the regulatory chain in the heterotropic mechanism of Escherichia coli aspartate transcarbamoylase On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin Expression and characterization of apolipoprotein(a) kringle IV types 1, 2 and 10 in mammalian cells Gene synthesis and functional expression of a protein exhibiting monodomain IgG Fc binding Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv Local polarity analysis: a sensitive method that discriminates between native proteins and incorrectly folded models Site-directed mutagenesis of a calcium binding site modifies specifically the different biochemical properties of annexin I A single Fc binding domain-alkaline phosphatase gene fusion expresses a protein with both IgG binding ability and alkaline phosphatase enzymatic activity Kinetic and equilibrium intermediates in protein folding The X-ray structure of (MeBm2t)1-cyclosporin complexed with cyclophilin A provides an explanation for its anomalously high immunosuppressive activity Secondary structure formation in model polypeptide chains

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