Method for the detection of a conformational state of a protein being in a complex mixture of further proteins and other biomolecules, wherein the protein has been subjected to a condition inducing a structural change, including: limited proteolysis of the extract mixture under a condition in which the protein is in the original conformational state to be detected leading to a first fragment sample; directly followed by (2) removal of large peptides and proteins or other biomolecules from said first fragment sample to form an enriched fragment sample; (3) analytical analysis of the enriched fragment sample for the determination of fragments characteristic of having been the result of the limited proteolysis of (1) as well as remaining after the removal (2) for the determination of the conformational state of said at least one protein.

An object of the invention is to provide a peptide having a stabilized secondary structure. The present invention provides a peptide having a secondary structure stabilized by a crosslinked structure and containing at least one combination of a special amino acid of the formula (I): ##STR00001##
(wherein, (A) represents a single bond or a linking group having, in the main chain thereof, from 1 to 10 atoms; (B) represents a group containing at least one bond; (C) represents a hydrogen atom or an alkyl group which may be substituted with a substituent; and X represents a group substitutable by a substitution reaction with a sulfanyl group) and an amino acid having, in the side chain thereof, a sulfanyl group; and having the crosslinked structure formed through a thioether bond between the side chain of the special amino acid residue and the sulfanyl group.

The invention provides an assay method for detection and/or quantification of a plurality of nucleic acid or protein targets in a sample. In the method probes are used to associate a detectable tag sequence with each of the selected targets present in the sample. Probes or primers sufficient to identify at least 25, and preferably at least 500, different targets are used. The method involves segregating aliquots of the sample from each other and detecting the tag sequences in each aliquot.

Embodiments of the present disclosure provide for -AApeptides, -AApeptide building blocks, methods of making -AApeptides and libraries of -AApeptides, methods of screening the -AApeptide libraries for desired peptidomimetic activity, and the like. The present disclosure also provides for -AApeptides that are inhibitors of A peptide aggregation, methods of inhibiting and disassembling A peptide aggregation, methods of inhibiting the toxicity of A aggregates towards N2a neuroblasotma cells, as well as methods and compounds for treating Alzheimer's disease.

A method for determining an interaction between a first protein and a second protein comprises the steps of: expressing in a cell or introducing into a cell a first fusion protein comprising the first protein, a multimerizable protein, and a fluorescent protein, and a second fusion protein comprising the second protein and a multimerizable protein; detecting a fluorescent focus formed by an association between the first fusion protein and the second fusion protein in the cell; and determining an interaction between the first protein and the second protein according to the detection of the fluorescent focus.

The present invention provides a system and method for assessing a synthetic peptide population including interrogating a population of peptide features in the presence of a receptor having an affinity for a binder sequence. The population of peptide features is synthesized over a plurality of synthesis periods and includes a plurality of control peptide features synthesized to have an amino acid sequence including the binder sequence. The control peptide features include a first feature synthesized beginning with a first one of the synthesis periods, and a second feature synthesized beginning after the first one of the synthesis periods such that synthesis of the second control peptide feature is delayed by at least one synthesis period. The method further includes detecting a signal output characteristic of an interaction of the receptor with the control peptide features, the signal output indicative of the fidelity of synthesis of the population of peptide features.

The present invention provides kits and assay methods for the early detection of pathogens, precise identification of the etiologic agent, and improved disease surveillance. More specifically, the present invention discloses an immunoassay leading to the rapid and simultaneous detection of antibodies to a wide range of infectious pathogens in biological fluids of infected patients. This immunoassay involves the covalent and oriented coupling of fusion proteins comprising an AGT enzyme and a viral antigen on an identifiable solid support (e.g. fluorescent microspheres), said support being previously coated with an AGT substrate. This coupling is mediated by the irreversible reaction of the AGT enzyme on its substrate. The thus obtained antigen-coupled microspheres show enhanced capture of specific antibodies as compared to antigen-coupled microspheres produced by standard amine coupling procedures. The methods of the invention possess the ability to multiplex, minimize the amount of biological sample, and have enhanced sensitivity and specificity toward target antibodies as compared with classical ELISA or Radio-Immunoprecipitation assays.

This disclosure relates to a method of generating conditionally active biologic proteins from wild type proteins, in particular therapeutic proteins, which are reversibly or irreversibly inactivated at the wild type normal physiological conditions. For example, evolved proteins are virtually inactive at body temperature, but are active at lower temperatures.

This disclosure relates to a method of generating conditionally active biologic proteins from wild type proteins, in particular therapeutic proteins, which are reversibly or irreversibly inactivated at the wild type normal physiological conditions. For example, evolved proteins are virtually inactive at body temperature, but are active at lower temperatures.

Water-soluble triazabutadiene molecules and methods for producing and using such compounds. The triazabutadiene molecules may be more labile at pH levels below physiological pH, such as pH 7, pH 6, pH 5, etc. The triazabutadiene molecules and compounds may be used for depositing diazonium salt and/or cargo in a pH-sensitive manner. The triazabutadiene molecules may alternatively be cleaved in reducing conditions or as a light-catalyzed reaction. The compounds herein may be used for delivery of drugs, as part of detection systems, or for other applications such as underwater adhesive applications.