Abstract: Polypeptides that comprise axle or ring components of protein nanomachines, and kits and nanomachines including such polypeptides are disclosed herein.

Abstract: Polypeptide are providing that are at least 50% identical to the amino acid sequence selected from the group consisting of SEQ ID NOS:1-37, cyclic homo-oligomers of the polypeptides, and uses thereof.

Abstract: The application discloses multimeric assemblies packaging one or more active component and their use to carry out nucleic acid regulation or gene editing.

Abstract: De novo designed proteins with binding activity are disclosed, which were designed starting from a desired functional site and jointly filling in the missing sequence and structure needed to complete the protein, and uses of the binding proteins.

Abstract: Cyclic peptides including the amino acid sequence selected from SEQ ID NO:1-6, multimers thereof, and metal organic frameworks including the cyclic peptides or multimers thereof are provided.

Abstract: Disclosed herein are designed heterodimer proteins, monomeric polypeptides capable of forming heterodimer proteins, protein scaffolds including such polypeptides, and methods for using the heterodimer proteins and subunit polypeptides for designing logic gates.

Abstract: The present invention relates to methods and compositions for the high throughput screening of protein-protein interactions in yeast liquid culture. Protein fusions non-native to yeast may be expressed to replace endogenous sexual agglutination proteins and mediate library-by-library interrogation of protein interactions. The methods and compositions of the invention can be utilized for the characterization of protein interaction networks in high throughput for both binding affinity and specificity, which is crucial for understanding cellular functions, screening therapeutic candidates, and evaluating engineered protein networks.

Abstract: The present disclosure provides human 1L-23R (WL-23R) binding polypeptides, conditionally maximally active SilL˜23R binding proteins, multimers thereof, and methods for using the polypeptides and binding proteins for therapeutic use.

Abstract: Beta-sheet forming polypeptides at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the amino acid sequence selected from the group consisting of SEQ ID NOS:1-24 are disclosed, together with their use and methods for designing beta-sheet forming polypeptides.

Abstract: Embodiments described herein improve fuel economy by controlling a vehicle powertrain based on a predicted vehicle velocity. The vehicle velocity is predicted based on vehicle-to-vehicle data when a prediction horizon is a longer prediction horizon and the vehicle velocity is predicted based on historical drive cycle data when the prediction horizon is a shorter prediction horizon. A time duration of the shorter prediction horizon is shorter than the time duration of the longer prediction horizon. A plurality of drive cycles are established for both the longer and the shorter prediction horizons using a neural network. A shorter prediction horizon drive cycle uses nonlinear autoregressive exogenous model neural networks and the longer prediction horizon drive cycle uses two layer feedforward neural networks. The predicted vehicle velocity is determined from a similar drive cycle of the plurality of drive cycles of either the shorter and/or the longer prediction horizon drive cycles.

Abstract: Polypeptides are disclosed comprising an (Fc) binding domain, a helical polypeptide monomer, and an oligomer domain, polymers thereof, and uses thereof.

Abstract: The application discloses multimeric assemblies including multiple oligomeric substructures, where each oligomeric substructure includes multiple proteins that self-interact around at least one axis of rotational symmetry, where each protein includes one or more polypeptide-polypeptide interface (“O interface”); and one or more polypeptide domain that is capable of effecting membrane scission and release of an enveloped multimeric assembly from a cell by recruiting the ESCRT machinery to the site of budding by binding to one or more proteins in the eukaryotic ESCRT complex (“L domain”); and where the multimeric assembly includes one or more subunits comprising one or more polypeptide domain that is capable of interacting with a lipid bilayer (“M domain”), as well as membrane-enveloped versions of the multimeric assemblies.

Abstract: Nanostructures and nanostructure-based vaccines that display antigens capable of eliciting immune responses to infectious agents such as bacteria, viruses, and pathogens are provided. Some vaccines are useful for preventing or decreasing the severity of infection with an infectious agent, including, for example and without limitation, lyme disease, pertussis, herpes virus, orthomyxovirus, paramyxovirus, pneumovirus, filovirus, flavivirus, reovirus, retrovirus, meningococcus, or malaria. The antigens may be attached to the core of the nanostructure either non-covalently or covalently, including as a fusion protein or by other means. Multimeric antigens may optionally be displayed along a symmetry axis of the nanostructure. Also provided are proteins and nucleic acid molecules encoding such proteins, vaccine compositions, and methods of administration.

Abstract: Disclosed herein are macrocyclic polypeptides having no more than 3 amino acid substitutions compared to the amino acid sequence of any one of SEQ ID NO: 1-2.37 or a mirror image thereof, wherein the polypeptide includes both L and D amino acids, libraries of such polypeptides, and uses thereof.

Abstract: Polypeptide are disclosed that comprise an amino acid sequence at least 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the amino acid sequence selected from the group consisting of SEQ ID NO:1-1615, not including any functional domains added fused to the protein (whether N-terminal, C-terminal, or internal), and wherein the 1, 2, 3, 4, or 5 N-terminal and/or C-terminal amino acid residues may be present or absent when considering the percent identity.

Abstract: The present disclosure provides non-naturally occurring beta barrel proteins as defined, self-complementing multipartite beta barrel proteins, uses of such proteins, and methods for designing such proteins.

Abstract: The disclosure provides two-dimensional protein structures including first and second polypeptides that are different, each form homo-oligomers, and interact to form a rigid interface, polypeptide components of such two-dimensional protein structures, and uses thereof.

Abstract: The disclosure provides polypeptide comprising or consisting of an amino acid sequence at least 66%, 70%, 75%, 80%, 82%, 84%, 86%, 88%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the amino acid sequence selected from the group consisting of SEQ ID NO: 1-91 as shown in Table I, wherein: (a) amino acid residues in upper case are L amino acids, and residues in lower case are D amino acids; (b) X is 2-aminoisobutyric acid (ATB); (c) no amino acid changes at proline or AIB e residues in the reference peptide are permitted; and (d) any amino acid changes must maintain chirality relative to the reference peptide.

Abstract: The disclosure provides antibody-like polypeptides of the formula X1-X2-X3-X4-X5-X6-X7-X8-X9-X10-X11-X12-X13-X14-X15, wherein the domains are as defined herein, nucleic acids encoding the polypeptides, and methods for use and design of the polypeptides.

Abstract: The disclosure provides cage proteins comprising a helical bundle, wherein the cage protein comprises a structural region and a latch region, wherein the latch region comprises one or more target binding polypeptide, wherein the cage protein further comprises a first reporter protein domain, wherein the first reporter protein domain undergoes a detectable change in reporting activity when bound to a second split reporter protein domain, and wherein the structural region interacts with the latch region to prevent solution access to the one or more target binding polypeptide.