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An amplified sensitivity arising from covalent modification in biological systems.
The transient and steady-state behavior of a reversible covalent modification system is examined, finding that amplification of the response to a stimulus can provide additional sensitivity in biological control, equivalent to that of allosteric proteins with high Hill coefficients.
Proceedings of the National Academy of Sciences of the United States of America. Annual subject and author indexes.
This dissertation aims to provide a history of web exceptionalism from 1989 to 2002, a period chosen in order to explore its roots as well as specific cases up to and including the year in which descriptions of “Web 2.0” began to circulate.
Application of a Theory of Enzyme Specificity to Protein Synthesis.
  • D. Koshland
  • Chemistry, Medicine
    Proceedings of the National Academy of Sciences…
  • 1 February 1958
The suggestion of Lipmann' that the energy required to drive this reaction to the right came from adenosine triphosphate has been supported by the extensive work and an analysis of why this linking of amino acids presents such formidable difficulties is revealing.
The gradient-sensing mechanism in bacterial chemotaxis.
  • R. Macnab, D. Koshland
  • Biology, Medicine
    Proceedings of the National Academy of Sciences…
  • 1 September 1972
It was found, however, that a sudden increase also elicits a response, namely supercoordinated swimming, which demonstrates that chemotaxis is achieved by modulation of the incidence of tumbling both above and below its steady-state value.
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand.
The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been
Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY.
The protein (Escherichia coli CheY) that controls the direction of flagellar rotation during bacterial chemotaxis has been shown to be phosphorylated on the aspartate 57 residue, indicating that the sequence and conformation of the protein is designed to achieve a rapid hydrolysis.
High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.
The conservation of the small angular change in vitro suggests that the inter-subunit rotation may have relevance to the understanding of the mechanism of transmembrane signal transduction in vivo.