Abstract: An amino acid-specific binder selectively binds to a binding amino acid. A binder complex selectively identifies the binding amino acid and includes an adjunct attached to the amino acid-specific binder. The adjunct includes a taggant, protein, substrate, or chemical modifier. Selectively identifying an N-terminal amino acid includes anchoring a C-terminal end; contacting an N-terminal amino acid of the anchored analyte with the binder complex; selectively binding when the N-terminal amino acid includes the binding amino acid; producing, by the taggant of the tagged complex, a taggant signal; detecting the taggant signal; and identifying the N-terminal amino acid based on the taggant signal.

Abstract: An amino acid-specific binder selectively binds to a binding amino acid. A binder complex selectively identifies the binding amino acid and includes an adjunct attached to the amino acid-specific binder. The adjunct includes a taggant, protein, substrate, or chemical modifier. Selectively identifying an N-terminal amino acid includes anchoring a C-terminal end; contacting an N-terminal amino acid of the anchored analyte with the binder complex; selectively binding when the N-terminal amino acid includes the binding amino acid; producing, by the taggant of the tagged complex, a taggant signal; detecting the taggant signal; and identifying the N-terminal amino acid based on the taggant signal.

Abstract: A di-enzymatic chimeric endolysin includes a primary enzymatic active domain including a primary protein sequence and that cleaves a glycosidic, peptide, or amide bond; a secondary enzymatic active domain disposed at a C-terminus end of the di-enzymatic chimeric endolysin and including a secondary protein sequence that, in combination with the primary enzymatic active domain, synergistically cleaves glycosidic, peptide, or amide bonds in a peptidoglycan; a cell wall binding domain including a recognition sequence that is sequentially interposed between the primary protein sequence and the secondary protein sequence and that binds to a cell wall; and a tertiary structure such that the primary enzymatic active domain faces and opposes the secondary enzymatic active domain in the di-enzymatic chimeric endolysin for synergistic cleavage of the peptidoglycan.

Abstract: An amino acid-specific binder selectively binds to a binding amino acid. A binder complex selectively identifies the binding amino acid and includes an adjunct attached to the amino acid-specific binder. The adjunct includes a taggant, protein, substrate, or chemical modifier. Selectively identifying an N-terminal amino acid includes anchoring a C-terminal end; contacting an N-terminal amino acid of the anchored analyte with the binder complex; selectively binding when the N-terminal amino acid includes the binding amino acid; producing, by the taggant of the tagged complex, a taggant signal; detecting the taggant signal; and identifying the N-terminal amino acid based on the taggant signal.

Abstract: An amino acid-specific binder selectively binds to a binding amino acid. A binder complex selectively identifies the binding amino acid and includes an adjunct attached to the amino acid-specific binder. The adjunct includes a taggant, protein, substrate, or chemical modifier. Selectively identifying an N-terminal amino acid includes anchoring a C-terminal end; contacting an N-terminal amino acid of the anchored analyte with the binder complex; selectively binding when the N-terminal amino acid includes the binding amino acid; producing, by the taggant of the tagged complex, a taggant signal; detecting the taggant signal; and identifying the N-terminal amino acid based on the taggant signal.

Abstract: An amino acid-specific binder selectively binds to a binding amino acid. A binder complex selectively identifies the binding amino acid and includes an adjunct attached to the amino acid-specific binder. The adjunct includes a taggant, protein, substrate, or chemical modifier. Selectively identifying an N-terminal amino acid includes anchoring a C-terminal end; contacting an N-terminal amino acid of the anchored analyte with the binder complex; selectively binding when the N-terminal amino acid includes the binding amino acid; producing, by the taggant of the tagged complex, a taggant signal; detecting the taggant signal; and identifying the N-terminal amino acid based on the taggant signal.

Abstract: A di-enzymatic chimeric endolysin includes a primary enzymatic active domain including a primary protein sequence and that cleaves a glycosidic, peptide, or amide bond; a secondary enzymatic active domain disposed at a C-terminus end of the di-enzymatic chimeric endolysin and including a secondary protein sequence that, in combination with the primary enzymatic active domain, synergistically cleaves glycosidic, peptide, or amide bonds in a peptidoglycan; a cell wall binding domain including a recognition sequence that is sequentially interposed between the primary protein sequence and the secondary protein sequence and that binds to a cell wall; and a tertiary structure such that the primary enzymatic active domain faces and opposes the secondary enzymatic active domain in the di-enzymatic chimeric endolysin for synergistic cleavage of the peptidoglycan.

Abstract: A process for making a nucleotide analog includes combining a first substrate that includes a linker and a base with a second substrate to form a substrate composition. An enzyme contacts the substrate composition and catalyzes formation of the nucleotide analog from the first substrate and the second substrate. Additionally, a composition includes the first substrate, second substrate, the enzyme, the nucleotide analog, and optional additives.

Abstract: A process for making a nucleotide analog includes combining a first substrate that includes a linker and a base with a second substrate to form a substrate composition. An enzyme contacts the substrate composition and catalyzes formation of the nucleotide analog from the first substrate and the second substrate. Additionally, a composition includes the first substrate, second substrate, the enzyme, the nucleotide analog, and optional additives.

Abstract: The present invention provides methods, compositions, and kits for detecting TC I deficiency in individuals with low serum cobalamin levels. Methods for detecting TCN1 mutations and/or the TC I isoforms or products of TCN1 mutations are useful for detecting and diagnosing those who have TC I deficiency and thereby can be said to have TC I deficiency instead of cobalamin deficiency.

Abstract: The present invention relates to a PCR method for generating a labeled double stranded nucleotide sequence that upon digestion with a restriction nuclease generates a double stranded nucleotide sequence having either a 3? or 5? overhang of a ssDNA sequence that can serve as helicase substrate.

Abstract: Disclosed is a method of determining alternatively spliced mRNAs by hybridization of mRNAs to exon/intron junction specific polynucleotide probes. Such polynucleotide probes allow the identification of alternative and aberrant splicing of known exons of a gene. These polynucleotide probes may by contained in DNA arrays to allow the screening of a large number of alternative and aberrant splicing variants.