A method for detecting an interaction between one or more protein bait and one or more candidate prey in a eukaryotic cell, comprising the steps of: a) providing an eukaryotic cell expressing (i) one or more protein bait, and (ii) one or more candidate prey, wherein said protein bait comprises a bait moiety and a polymerized-tubulin binding moiety. b) determining the occurence of an interaction between said one or more protein bait and said one or more candidate prey in the eukaryotic cell, wherein said protein bait is bound to polymerized tubulin in the eukaryotic cell, thereby localizing said one or more candidate prey along said polymerized tubulin, thereby detecting said interaction.

An isolated nucleic acid that includes an open reading frame encoding a lanthipeptide protease polypeptide for scarless tag removal from a polypeptide is presented. Reagents, expression constructs and methods are also provided for preparing a scarless tag polypeptide product from a tagged polypeptide precursor containing a lanthipeptide protease cleavage site. The reagents are directed to novel lanthipeptide proteases and expression constructs and polypeptide precursors that include highly specific lanthipeptide protease substrate recognition sequence. Methods are provided that enable scarless tag removal from a cognate lanthipeptide, a non-cognate lanthipeptide or a heterologous polypeptide that includes extraneous amino acid sequences, such as leader peptides and tags.

Disclosed is a method for purifying a target protein, comprising steps of: bringing a fusion protein containing an amino acid sequence of a peptide tag, an amino acid sequence of a cleavable site of a protease and an amino acid sequence of a target protein, into contact with the protease in a solution, to cleave the peptide tag from the fusion protein; and bringing the solution containing the peptide tag, the target protein and the protease into contact with an ion exchange resin to separate the target protein and the peptide tag, thereby acquiring a solution containing the target protein, wherein, in the fusion protein, the amino acid sequence of a cleavable site of the protease exists between the amino acid sequence of the peptide tag and the amino acid sequence of the target protein, and the peptide tag is polyanionic or polycationic.

Provided are a baicalein- and scutellarein-synthesizing microorganism, a preparation method for same, and applications thereof. By modifying a heterologous metabolic pathway of a host cell per a genetic engineering method, acquired is an engineered strain providing a high yield of baicalein and scutellarein. Also provided is a process for utilizing the engineered strain to produce baicalein and scutellarein.

Provided herein are lasso peptides libraries, and particularly molecular display libraries of lasso peptides. Also provided herein are related methods and systems for producing the libraries and for screening the libraries to identify candidate lasso peptides having desirable properties.

The disclosure relates to a virus-like particle in which a protein complex is entrapped, ensuring the formation of the protein complex under physiological conditions, while protecting the protein complex during purification and identification. The disclosure further relates to the use of such virus-like particle for the isolation and identification of protein complexes.

The invention relates to proximity-based sortase-mediated protein purification and ligation. Specifically, the invention relates to techniques that links protein expression/purification with conjugation to therapeutic agents, imaging agents, or linkers.

Methods to prepare recombinant adeno-associated virus (AAV) capsids with altered tropism and compositions having AAVs with altered tropism are provided.

The present disclosure provides, inter alia, genetically encoded recombinant peptide biosensors comprising analyte-binding framework portions and signaling portions, wherein the signaling portions are present within the framework portions at sites or amino acid positions that undergo a conformational change upon interaction of the framework portion with an analyte.

The present invention relates to polypeptides comprising a carbohydrate-binding module amino acid sequence and an alpha-amylase amino acid sequence as well as to the application of such polypeptides.