A method of macrocyclization of peptidomimetics is described which comprises substitution of one or more of the backbone amide C═O bonds with a turn-inducing motif. The method is general with enhancements seen across a range of ring sizes (e.g. tri-, tetra-, penta- and hexapeptides). Specifically, a peptidomimetic macrocycle is described comprising a carbonyl bioisosteric turn-inducing element having the structure: ##STR00001## wherein X is a heteroatom; and wherein R.sub.1 to R.sub.6 are each independently selected from alkyl, aryl, heteroaryl and H.

A device for processing samples is disclosed. Interior surfaces of the device, which come in contact with fluids, define wetted surfaces. A portion of the wetted surfaces are coated with an alkylsilyl coating having the Formula I: ##STR00001##
R.sup.1, R.sup.2, R.sup.3, R.sup.4, R.sup.5, and R.sup.6 are each independently selected from (C.sub.1-C.sub.6)alkoxy, —NH(C.sub.1-C.sub.6)alkyl, —N((C.sub.1-C.sub.6)alkyl).sub.2, OH, OR.sup.A, and halo. R.sup.A represents a point of attachment to the interior surfaces of the fluidic system. At least one of R.sup.1, R.sup.2, R.sup.3, R.sup.4, R.sup.5, and R.sup.6 is OR.sup.A. X is (C.sub.1-C.sub.20)alkyl, —O[(CH.sub.2).sub.2O].sub.1-20—, —(C.sub.1-C.sub.10)[NH(CO)NH(C.sub.1-C.sub.10)].sub.1-20—, or —(C.sub.1-C.sub.10)[alkylphenyl(C.sub.1-C.sub.10)alkyl].sub.1-20—.

A method for measuring radiation intensity includes measuring the radiation intensity received by the protein in a radiation field based on degree of protein degradation in the radiation field, wherein the degree of degradation is a ratio of the molecular weight of the protein before and after irradiation. The measuring method is simple in operation, small in number of steps, small in error, and capable of measuring radiation doses of various radiation fields or even mixed radiation fields. Use of a biological dosimeter for measuring the radiation intensity by the method in a neutron capture therapy system can not only assess radiation contamination in the irradiation chamber, but also evaluate the neutron dose.

Provided herein are methods for preparing biological samples for spatial proteomic analysis, methods of determining a location of a protein analyte in a biological sample, and methods of determining a location of a protein analyte and a nucleic acid analyte in a biological sample.

The invention provides assays and methods for diagnosing and treating infectious diseases. The invention relates in some embodiments to urinary biomarkers and their use in the differential diagnosis of bacterial and viral infections. The invention further relates to means for determining and providing correct treatment to infection in a non-invasive manner, while minimizing antibiotic misuse.

Disclosed herein include methods, compositions, and kits suitable for use in detecting the activation level of a signal transducer. In some embodiments, there are provided synthetic protein circuits wherein recruitment of synthetic protein circuit components to an association location upon activation of a signal transducer generates an active effector protein. The effector protein can be configured to carry out a variety of functions when in an active state, such as, for example, inducing cell death. Methods of treating a disease or disorder characterized by aberrant signaling are provided in some embodiments.

The invention encompasses methods and test strips for detecting the presence of cerebrospinal fluid (CSF) in a biological sample with a lateral flow device which uses lectin conjugates, anti-antigen conjugates, an immobilized serum line, and an immobilized anti-antigen line.

Provided is a method for simply obtaining a desired size fraction from an aqueous sample containing particles. The method includes the following steps: (1) bringing the aqueous sample containing particles into contact with a superabsorbent polymer to obtain a superabsorbent polymer gel containing a portion of the particles, and (2) mixing the superabsorbent polymer gel with a salt to recover a portion of the particles.

Apparatus and methods for the detection of proteins in biological fluids such as urine using a label-free assay is described. Specific proteins are detected by their binding to highly specific capture reagents such as SOMAmers that are attached to the surface of a substrate. Changes to these capture reagents and their local environment upon protein binding modify the behavior of color centers (e.g., fluorescence, ionization state, spin state, etc.) embedded in the substrate beneath the bound capture reagents. These changes can be read out, for example, optically or electrically, for an individual color center or as an average response of many color centers.

The present disclosure provides a system comprising a communication interface and computer for assigning a label to the biomolecule fingerprint, wherein the label corresponds to a biological state. The present disclosure also provides a sensor arrays for detecting biomolecules and methods of use. In some embodiments, the sensor arrays are capable of determining a disease state in a subject.