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.
Comparison of experimental binding data and theoretical models in proteins containing subunits.
Application of a Theory of Enzyme Specificity to Protein Synthesis.
- D. Koshland
- Biology, ChemistryProceedings 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.
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…
Amplification and adaptation in regulatory and sensory systems.
STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS
- D. Koshland
- 1 November 1953
High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.
- Joanne I. Yeh, H. Biemann, G. Privé, J. Pandit, D. Koshland, S. Kim
- ChemistryJournal of Molecular Biology
- 20 September 1996
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.
Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.
The coenzyme-binding site confirms the fundamentally different evolution of the isocitrate dehydrogenase-like and the lactate dehydrogenases-like classes of nucleotide-binding proteins.