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Frederick Dahlquist
Frederick Dahlquist
Unknown affiliation
Verified email at chem.ucsb.edu
Title
Cited by
Cited by
Year
pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
DE Anderson, WJ Becktel, FW Dahlquist
Biochemistry 29 (9), 2403-2408, 1990
7221990
[3] Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
DC Muchmore, LP McIntosh, CB Russell, DE Anderson, FW Dahlquist
Methods in enzymology 177, 44-73, 1989
6481989
Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution
DA Hall, DC Maus, GJ Gerfen, SJ Inati, LR Becerra, FW Dahlquist, ...
Science 276 (5314), 930-932, 1997
5891997
Studying excited states of proteins by NMR spectroscopy
FAA Mulder, A Mittermaier, B Hon, FW Dahlquist, LE Kay
Nature structural biology 8 (11), 932-935, 2001
4962001
Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
JA Gegner, DR Graham, AF Roth, FW Dahlquist
Cell 70 (6), 975-982, 1992
4801992
[13] The meaning of scatchard and hill plots
FW Dahlquist
Methods in enzymology 48, 270-299, 1978
4001978
Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy:  Application to Asn and Gln …
FAA Mulder, NR Skrynnikov, B Hon, FW Dahlquist, LE Kay
Journal of the American Chemical Society 123 (5), 967-975, 2001
3682001
Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins
LP McIntosh, FW Dahlquist
Quarterly reviews of biophysics 23 (1), 1-38, 1990
3351990
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
G Bouvignies, P Vallurupalli, DF Hansen, BE Correia, O Lange, A Bah, ...
Nature 477 (7362), 111-114, 2011
3092011
Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme
S Dao-Pin, DE Anderson, WA Baase, FW Dahlquist, BW Matthews
Biochemistry 30 (49), 11521-11529, 1991
2871991
Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA.
JA Gegner, FW Dahlquist
Proceedings of the National Academy of Sciences 88 (3), 750-754, 1991
2641991
Quantitative analysis of bacterial migration in chemotaxis
FW Dahlquist, P Lovely, DE Koshland
Nature New Biology 236 (65), 120-123, 1972
2591972
The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28
GW Daughdrill, MS Chadsey, JE Karlinsey, KT Hughes, FW Dahlquist
Nature structural biology 4 (4), 285-291, 1997
2571997
Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme
G Yang, C Cecconi, WA Baase, IR Vetter, WA Breyer, JA Haack, ...
Proceedings of the National Academy of Sciences 97 (1), 139-144, 2000
2542000
Statistical measures of bacterial motility and chemotaxis
PS Lovely, FW Dahlquist
Journal of theoretical biology 50 (2), 477-496, 1975
2491975
An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H-labeled proteins: application to a 37-kDa Trp repressor-DNA complex
T Yamazaki, W Lee, M Revington, DL Mattiello, FW Dahlquist, ...
Journal of the American Chemical Society 116 (14), 6464-6465, 1994
2301994
Reconstructing NMR spectra of “invisible” excited protein states using HSQC and HMQC experiments
NR Skrynnikov, FW Dahlquist, LE Kay
Journal of the American Chemical Society 124 (41), 12352-12360, 2002
2292002
The amide nitrogen-15 chemical shift tensors of four peptides determined from carbon-13 dipole-coupled chemical shift powder patterns
TG Oas, CJ Hartzell, FW Dahlquist, GP Drobny
Journal of the American Chemical Society 109 (20), 5962-5966, 1987
2211987
Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
S Wilkens, FW Dahlquist, LP McIntosh, LW Donaldson, RA Capaldi
Nature structural biology 2 (11), 961-967, 1995
2181995
Structural basis for the attachment of a paramyxoviral polymerase to its template
RL Kingston, DJ Hamel, LS Gay, FW Dahlquist, BW Matthews
Proceedings of the National Academy of Sciences 101 (22), 8301-8306, 2004
2172004
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