Authors:
Giesen, AW
Bae, LC
Barrett, CL
Chyba, JA
Chaykovsky, MM
Cheng, MC
Murray, JH
Oliver, EJ
Sullivan, SM
Brown, JM
Dahlquist, FW
Homans, SW
Citation: Aw. Giesen et al., Measurement of one-bond H-1(alpha)-C-13(alpha) couplings in backbone-labelled proteins, J BIOM NMR, 19(3), 2001, pp. 255-260
Authors:
Goto, NK
Skrynnikov, NR
Dahlquist, FW
Kay, LE
Citation: Nk. Goto et al., What is the average conformation of bacteriophage T4 lysozyme in solution?A domain orientation study using dipolar couplings measured by solution NMR, J MOL BIOL, 308(4), 2001, pp. 745-764
Citation: Wa. Deutschman et Fw. Dahlquist, Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima, BIOCHEM, 40(43), 2001, pp. 13107-13113
Authors:
Ryan, M
Liu, T
Dahlquist, FW
Griffith, OH
Citation: M. Ryan et al., A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C, BIOCHEM, 40(32), 2001, pp. 9743-9750
Authors:
Mulder, FAA
Skrynnikov, NR
Hon, B
Dahlquist, FW
Kay, LE
Citation: Faa. Mulder et al., Measurement of slow (mu s-ms) time scale dynamics in protein side chains by N-15 relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme, J AM CHEM S, 123(5), 2001, pp. 967-975
Authors:
Skrynnikov, NR
Mulder, FAA
Hon, B
Dahlquist, FW
Kay, LE
Citation: Nr. Skrynnikov et al., Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme, J AM CHEM S, 123(19), 2001, pp. 4556-4566
Citation: D. Barrick et Fw. Dahlquist, Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion, PROTEINS, 39(4), 2000, pp. 278-290
Authors:
Mulder, FAA
Hon, B
Muhandiram, DR
Dahlquist, FW
Kay, LE
Citation: Faa. Mulder et al., Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR, BIOCHEM, 39(41), 2000, pp. 12614-12622
Authors:
Anderson, JS
Forman, MD
Modleski, S
Dahlquist, FW
Baxter, SM
Citation: Js. Anderson et al., Cooperative ordering in homeodomain-DNA recognition: Solution structure and dynamics of the MATa1 homeodomain, BIOCHEM, 39(33), 2000, pp. 10045-10054
Authors:
Halkides, CJ
McEvoy, MM
Casper, E
Matsumura, P
Volz, K
Dahlquist, FW
Citation: Cj. Halkides et al., The 1.9 angstrom resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY, BIOCHEM, 39(18), 2000, pp. 5280-5286
Authors:
McEvoy, MM
Bren, A
Eisenbach, M
Dahlquist, FW
Citation: Mm. Mcevoy et al., Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM, J MOL BIOL, 289(5), 1999, pp. 1423-1433
Authors:
Gassner, NC
Baase, WA
Lindstrom, JD
Lu, JR
Dahlquist, FW
Matthews, BW
Citation: Nc. Gassner et al., Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding, BIOCHEM, 38(44), 1999, pp. 14451-14460