Abstract: The invention relates to modified proteins of the superfamily of “ubiquitin-like proteins”, proteins that have a ubiquitin-like fold and fragments or fusion proteins thereof. As a result of said modification, the proteins have a binding affinity with respect to a predetermined binding partner that did not exist previously. The invention also relates to a method for the production and utilization of said proteins.

Abstract: The invention relates to modified proteins of the superfamily of “ubiquitin-like proteins”, proteins that have a ubiquitin-like fold and fragments or fusion proteins thereof. As a result of said modification, the proteins have a binding affinity with respect to a predetermined binding partner that did not exist previously. The invention also relates to a method for the production and utilization of said proteins.

Abstract: The present invention describes novel beta-sheet proteins having specific binding properties and catalytic properties and also methods for preparing these proteins.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: The present invention describes novel beta-sheet proteins having specific binding properties and catalytic properties and also methods for preparing these proteins.

Abstract: The invention relates to modified proteins of the superfamily of “ubiquitin-like proteins”, proteins that have a ubiquitin-like fold and fragments or fusion proteins thereof. As a result of said modification, the proteins have a binding affinity with respect to a predetermined binding partner that did not exist previously. The invention also relates to a method for the production and utilization of said proteins.

Abstract: In order to recombinantly prepare a biologically active protein of the TGF-? superfamily, a protein, whose amino terminus consists of the pro sequence of a protein of the TGF-? superfamily, or parts thereof, to which the mature domain of this protein or of another protein of TGF-? superfamily which exhibits at least 35% homology with mature BMP-2 is attached, is expressed in prokaryotes under conditions in which at least a part of the protein is obtained in the form of inclusion bodies, the inclusion bodies are isolated and solubilized under denaturing conditions, the denatured, monomeric and biologically inactive protein which has been solubilized from the inclusion bodies is renatured, with folding and dimerization to give the soluble, biologically active conformation and, where appropriate, after the renaturation, the mature protein is released proteolytically from its pro form.

Abstract: The present invention describes novel beta-sheet proteins having specific binding properties and catalytic properties and also methods for preparing these proteins.

Abstract: The invention concerns recombinant proteinase K. Furthermore a method for producing recombinant proteinase K is disclosed, which is characterized in that a) a host cell is transformed with a recombinant nucleic acid which codes for the zymogenic precursor of proteinase K, b) the host cell is cultured in such a manner that the zymogenic precursor of proteinase K is formed in the form of inclusion bodies in the host cell, c) the inclusion bodies are isolated and natured under conditions which result in the formation of the protease part of the zymogenic precursor in its natural conformation, d) the natured proteinase K is activated and purified.

Abstract: The present invention relates to a method for the synthesis of peptides, peptide mimetics and/or proteins and/or for the selective N-terminal modification of peptides, peptide mimetics and/or proteins, with the steps of: a) providing an amino component, said amino component having at least one amino acid, b) providing a carboxyl component, said carboxyl component having a leaving group on the carboxyl group, and said carboxyl component being a compound having at least one amino acid or a compound having at least one label or reporter group, c) reacting said amino component and said carboxyl component in a reaction medium which has one or more ionic liquids, in the presence of a protease, peptidase and/or hydrolase, to form a peptide bond between the amino component and the carboxyl component with elimination of the leaving group.

Abstract: The invention relates to modified proteins of the superfamily of “ubiguitin-like proteins”, proteins that have a ubiguitin-like fold and fragments or fusion proteins thereof. As a result of said modification, the proteins have a binding affinity with respect to a predetermined binding partner that did not exist previously. The invention also relates to a method for the production and utilization of said proteins.

Abstract: The invention relates to transport systems for molecular substances, comprising a mosaic of recombinant partial units (individual components). The invention further relates to production of the molecular transport system and use thereof.

Abstract: The present invention relates to the use of substituted imidazolium salts for the renaturation, for the decrease of aggregation and/or for the increase of the thermal stability of proteins as well as to a method for the renaturation of proteins, for the decrease of the aggregation and/or for the increase of the thermal stability of proteins as well as to renatured proteins prepared by means of the method according to the invention. In the method according to the invention, the proteins to be treated are contacted with a liquid renaturation medium containing substituted imidazolium salts.

Abstract: In order to recombinantly prepare a biologically active protein of the TGF-&bgr; superfamily, a protein, whose amino terminus consists of the pro sequence of a protein of the TGF-&bgr; superfamily, or parts thereof, to which the mature domain of this protein or of another protein of TGF-&bgr; superfamily which exhibits at least 35% homology with mature BMP-2 is attached, is expressed in prokaryotes under conditions in which at least a part of the protein is obtained in the form of inclusion bodies, the inclusion bodies are isolated and solubilized under denaturing conditions, the denatured, monomeric and biologically inactive protein which has been solubilized from the inclusion bodies is renatured, with folding and dimerization to give the soluble, biologically active conformation and, where appropriate, after the renaturation, the mature protein is released proteolytically from its pro form.

Abstract: A process for the production of a naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges by a) culturing prokaryotic cells in which the said prokaryotic cells contain an expression vector which codes for the said polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) secreting the polypeptide into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium, which is characterized in that a nucleic acid coding for a molecular chaperone is additionally expressed in the said prokaryotic cell and the chaperone is secreted into the periplasm, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.

Abstract: A chimeric polypeptide has a first and a second polypeptide chain chemically linked via 1 to 3 cysteine-based disulfide bridges. The first polypeptide chain consists of 1 to 3 cysteines and 4 to 12 basic amino acids preferably selected from the group consisting of arginine, lysine and ornithine. The second polypeptide chain consists of 1 to 3 cysteines and 4 to 12 acidic amino acids selected from the group consisting of glutamate and aspartate. Each polypeptide chain is linked at its C- or N-terminus to a biologically active compound, and is useful as a multimeric pharmaceutical agent.

Abstract: The invention concerns a process for increasing the formation of the natural protein conformation when disulfide-bonded proteins are secreted by a prokaryotic host organism that contains a recombinant DNA coding for the secreted protein whereby the host organism is cultured in a suitable culture medium under suitable conditions for the expression of the recombinant DNA, which is characterized in that a culture medium containing 0.1 to 20 mmol/l of one or several thiol reagents is used.

Abstract: A process produces a water-soluble, naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges. This process involves culturing prokaryotic cells, a) in which the prokaryotic cells contain an expression vector which encodes the polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) under conditions under which the polypeptide is secreted into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium. In this process, the culturing is carried out in the presence of arginine or a compound of the formula I R2—CO—NR1 (I) in which R and R1 represent hydrogen or a saturated or unsaturated branched or unbranched C1-C4 alkyl chain and R2 represents hydrogen, NHR1 or a saturated or unsaturated branched or unbranched C1-C3 alkyl chain, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.