Systems and methods for modeling a three-dimensional protein structure are disclosed. The method includes receiving a primary amino acid sequence of a three-dimensional protein, translating the primary amino acid sequence to a first vector, determining a per-residue conformation index for each amino acid residue in the primary amino acid sequence, determining a vector set for each amino acid residue in the primary amino acid sequence, and using the per-residue interaction vector set to generate a multi-dimensional matrix for the three-dimensional protein structure. The first vector includes a unique numerical descriptor value corresponding to each amino acid residue in the primary amino acid sequence. The vector set includes a plurality per-residue interaction factors corresponding to a plurality of conformation indexes for that amino acid residue.

The invention provides a fusion protein comprising, from N-terminus to C-terminus: a) a first portion of a Family B G-protein coupled receptor (GPCR) that comprises transmembrane helix (TM)-1, TM2 and TM3 of the GPCR; b) a stable protein domain; and c) a second portion of the GPCR comprising TM4, TM5, TM6 and TM7 of the GPCR. The invention also provides a method of crystallising a GPCR comprising providing the fusion protein of the invention and crystallising it to obtain crystals.

A chromatography device for removing a solute from a fluid is provided. The device has a first plate having an inlet and a first channel. The first channel directs the fluid from the inlet towards chromatographic media housed in a chamber coupled to the first plate. The chamber has a leading edge for receiving the fluid from the first channel and a trailing edge for delivering the fluid to a second channel. The chromatographic media is configured to remove the solute from the fluid as the fluid passes through the chamber. The device also has a second plate coupled to the chamber having the second channel and an outlet. The second channel directs the fluid from the chamber to the outlet. The direction of flow of fluid through the first channel and the second channel is transverse to a direction of flow of the fluid through the chromatographic media. A method of removing a solute from a fluid is also provided.

The present disclosure provides methods and compositions useful for the prophylactic and therapeutic amelioration and treatment of infections caused by Gram-negative bacteria, including Pseudomonas aeruginosa. The disclosure further provides compositions and methods of incorporating and utilizing lysin polypeptides of the present disclosure for augmenting the efficacy of antibiotics generally suitable for the treatment of Gram-negative bacterial infection.

The present invention provides RNA-guided gene editing systems and methods of use thereof.

This document relates to conjugates of a biologically active molecule or a derivative thereof and functionalized (e.g., mono- or bi-functional) polymers (e.g., polyethylene glycol and related polymers) as well as methods and materials for making and using such conjugates.

Some embodiments provide methods and systems for creating ladder/standards as quality control tools for length-based separation of carbon nanotubes; determining the length purity; or measuring distribution of lengths of a collection of carbon nanotubes. Some embodiments further provide methods and systems for dispersing carbon nanotubes by conjugation of the carbon nanotubes with biomolecule moieties, specifically proteins. Further, some embodiments provide an indicator for length-based separation of carbon nanotubes via conjugation of one or more biomolecules onto the surfaces of the nanotubes. In some embodiments, such a method can include conjugating a biomolecule to the carbon nanotubes and subjecting the conjugated carbon nanotubes to silver-stained gel electrophoresis to separate the conjugated carbon nanotubes based on their lengths.

The present disclosure is directed to a lysin-AMP polypeptide construct comprising: (a) a first component comprising the polypeptide sequence of: (i) SEQ ID NO: 118 (GN202); or (ii) a polypeptide having lysin activity and having at least 80% sequence identity with the polypeptide sequence of SEQ ID NO: 118 (GN202); or (iii) an active fragment of SEQ ID NO: 118 (GN202); and (b) a second component comprising the polypeptide sequence of at least one antimicrobial peptide (AMP), wherein the at least one AMP comprises SEQ ID NO: 114 (FIRL). Exemplary lysin-AMP polypeptides, such as GN370 (SEQ ID NO: 44) as well as methods of treating bacterial infections using the present lysin-AMP polypeptide constructs are also disclosed.

The present invention relates to novel methods of generating and screening for chimeric polypeptides, which can be used in the treatment and prophylaxis of pathogenic bacterial contamination, colonisation and infection. The novel methods are based on random recombination of protein domains, and the chimeric polypeptides obtainable by the methods according to the invention are characterized in that they comprise at least one enzymatic active domain (EAD) and at least one cell binding domain (CBD). The present invention also relates to a library of chimeric polypeptides obtainable by the methods of the present invention.

This document relates to conjugates of TNF inhibitors or derivatives thereof and functionalized (e.g., mono- or bi-functional) polymers (e.g., polyethylene glycol and related polymers) as well as methods and materials for making and using such conjugates.