(Q28364597)

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A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association

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scholarly article

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A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association (English)

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1 reference

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author name string

T N Luong

1

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J F Kirsch

2

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publication date

March 2001

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Protein Science

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10

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3

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581-91

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Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase

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Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase

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Altering the context of an RNA bulge switches the binding specificities of two viral Tat proteins

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A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids

1 reference

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Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis

1 reference

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Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine

1 reference

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Additivity of mutational effects in proteins

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Interconversion of the ligand arrays in the CD and EF sites of oncomodulin. Influence on Ca2+-binding affinity.

1 reference

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Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

1 reference

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12 December 2020

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inferred from PubMed ID database lookup

Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1110/PS.24101

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