The present invention relates to a peptide hormone with one or more O-glycans attached at specific amino acid residues as well as to formulations comprising the same.

Disclosed are compositions, methods, and kits for performing cell-free RNA transcription and/or cell-free protein synthesis (CFPS). The disclosed compositions, methods, and kits include or utilize components prepared from Vibrio species such as cellular extracts from Vibrio natriegens.

Disclosed are compositions, methods, and kits for performing cell-free RNA transcription and/or cell-free protein synthesis (CFPS). The disclosed compositions, methods, and kits include or utilize components prepared from Vibrio species such as cellular extracts from Vibrio natriegens.

The invention describes peptide ligands specific for human plasma Kallikrein.

The invention describes peptide ligands specific for human plasma Kallikrein.

Systems, methods and non-transitory computer readable media identify favored polymer conformations. One or more residues are identified and may be replaced in the polymer, or the original primary sequence of the polymer may be retained. The conformations of residues in a subset of residues in a region of the identified one or more residues are altered. This conformational adjustment is repeated for other subsets of residues in the region of the identified one or more residues, and for other conformations, thereby deriving a plurality of polymer structures. A set of clusters is generated for each residue of the polymer using the conformationally adjusted structures, thereby creating sets of clusters. Structures in the plurality of structures are grouped into subgroups when the structures fall into the same clusters across a threshold number of the sets of clusters. One or more physical properties are determined for structures in subgroups, thereby identifying one or more thermodynamically relevant polymer conformations for the polymer.

Systems, methods and non-transitory computer readable media identify favored polymer conformations. One or more residues are identified and may be replaced in the polymer, or the original primary sequence of the polymer may be retained. The conformations of residues in a subset of residues in a region of the identified one or more residues are altered. This conformational adjustment is repeated for other subsets of residues in the region of the identified one or more residues, and for other conformations, thereby deriving a plurality of polymer structures. A set of clusters is generated for each residue of the polymer using the conformationally adjusted structures, thereby creating sets of clusters. Structures in the plurality of structures are grouped into subgroups when the structures fall into the same clusters across a threshold number of the sets of clusters. One or more physical properties are determined for structures in subgroups, thereby identifying one or more thermodynamically relevant polymer conformations for the polymer.

A method for preparing interleukin-2 or an interleukin-2 analogue formed by at least three building blocks includes: synthesizing the at least three building blocks, whereby for each building block the C-terminal residue comprises an α-keto group and/or the N-terminal residue comprises a cyclic hydroxylamine; coupling the at least three building blocks by KAHA ligation resulting in a depsipeptide; and rearranging the depsipeptide to obtain interleukin-2 or an interleukin-2 analogue.

The present invention relates to a method of preparing a lysine side-chain modified peptide by solid phase peptide synthesis.

Disclosed in the present invention are an antibody targeting LAG-3, a preparation method therefor and the use thereof. In particular, disclosed in the present invention is a novel monoclonal antibody targeting LAG-3. Also disclosed in the present invention is a method for the preparation of the monoclonal antibody. The monoclonal antibody of the present invention is capable of binding LAG-3 antigens with high specificity, and has very high affinity and significant activities such as anti-tumor activity.