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Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
The results demonstrate that modulation of the kinase activity does not require association-dissociation of the ternary complex, which suggests that the receptor signal is transduced through conformational changes in the teranary complex rather than through changes of the association of the Kinase CheA with receptor and/or CheW.
Structural basis for the attachment of a paramyxoviral polymerase to its template.
- R. Kingston, Damon J. Hamel, L. Gay, F. Dahlquist, B. Matthews
- Biology, MedicineProceedings of the National Academy of Sciences…
- 1 June 2004
This study provides a structural analysis of polymerase-template interactions in a paramyxovirus and presents an example of a protein-protein interaction that must be only transiently maintained as part of its normal function.
Studying excited states of proteins by NMR spectroscopy
- F. Mulder, A. Mittermaier, B. Hon, F. Dahlquist, L. Kay
- Chemistry, MedicineNature Structural Biology
- 1 November 2001
Novel relaxation dispersion NMR techniques are used to kinetically and thermodynamically characterize a transition between a highly populated ground state conformation and an excited state that is 2.0 kcal mol−1 higher in free energy.
pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.
A mechanism of acid denaturation in which the unfolded state is progressively stabilized by protonation of its acid residues as pH is lowered below pH 4.5 is suggested.
Statistical measures of bacterial motility and chemotaxis.
A model for the three-dimensional microscopic behavior of motile bacteria is presented, and its parameters to five practical measures of bacterial motility and chemotaxis (direction correlation function, diffusion constant, persistence time, average velocity, and up/down ratio).
Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.
- G. Yang, C. Cecconi, +6 authors C. Bustamante
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 4 January 2000
A method of synthesizing polymers of protein molecules in the solid state by introducing cysteines at locations where bacteriophage T4 lysozyme molecules contact each other in a crystal and taking advantage of the alignment provided by the lattice is developed.
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
- F. Mulder, N. Skrynnikov, B. Hon, F. Dahlquist, L. Kay
- Chemistry, MedicineJournal of the American Chemical Society
- 16 January 2001
It is shown that many of the side chain amide groups of Asn and Gln residues in the C-terminal domain of the protein are affected by a chemical exchange process which may be important in facilitating the rapid binding of hydrophobic ligands to the cavity.
CheW Binding Interactions with CheA and Tar
- M. Boukhvalova, F. Dahlquist, R. Stewart
- Medicine, BiologyThe Journal of Biological Chemistry
- 21 June 2002
The results indicate that mutations which eliminate CheW binding to Tar or to CheA result in a complete inability to form active ternary complexes in vitro and render the CheW protein incapable of mediating chemotaxis in vivo.
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
The results suggest a mechanism for the evolution of a protein’s function by changing the delicate balance between the states on its energy landscape by inverting the relative populations of the ground and excited states and altering function.
The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28
- G. Daughdrill, M. Chadsey, J. Karlinsey, K. Hughes, F. Dahlquist
- Biology, MedicineNature Structural Biology
- 1 April 1997
The interaction between the flagellum specific sigma factor, σ28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR to postulate that the lack of structure in free and bound Flgm is important to its role as an exported protein.