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Showing 1–16 of 16 results

Advanced filters: Author: Frederick W. Dahlquist Clear advanced filters

Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface

Ronald V. Swanson
David F. Lowry
Frederick W. Dahlquist
Research01 Oct 1995
Nature Structural Biology

Volume: 2, P: 906-910
Access of ligands to cavities within the core of a protein is rapid

Victoria A. Feher
Enoch P. Baldwin
Frederick W. Dahlquist
Research01 Jun 1996
Nature Structural Biology

Volume: 3, P: 516-521
Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

Stephan Wilkens
Frederick W. Dahlquist
Roderick A. Capaldi
Research01 Nov 1995
Nature Structural Biology

Volume: 2, P: 961-967
Large modular proteins by NMR

Megan M. McEvoy
Aida Flor A. de la Cruz
Frederick W. Dahlquist
Comments & Opinion01 Jan 1997
Nature Structural Biology

Volume: 4, P: 9
How amino-acid insertions are allowed in an α-helix of T4 lysozyme

Dirk W. Heinz
Walter A. Baase
Brian W. Matthews
Research11 Feb 1993
Nature

Volume: 361, P: 561-564
A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin

Doug Barrick
Nancy T. Ho
Chien Ho
Research01 Jan 1997
Nature Structural Biology

Volume: 4, P: 78-83
Solution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase

NMR studies of the δ subunit of the Escherichia coli F₁F₀-ATPsynthase reveal that it consists of an N-terminal six α-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F₁ and F₀.

Stephan Wilkens
Stanley D. Dunn
Roderick A. Capaldi
Correspondence01 Mar 1997
Nature Structural Biology

Volume: 4, P: 198-201
The energetics of T4 lysozyme reveal a hierarchy of conformations

Manuel Llinás
Blake Gillespie
Susan Marqusee
Research01 Nov 1999
Nature Structural Biology

Volume: 6, P: 1072-1078
The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ²⁸

Gary W. Daughdrill
Meggen S. Chadsey
Frederick W. Dahlquist
Research01 Apr 1997
Nature Structural Biology

Volume: 4, P: 285-291
Studying excited states of proteins by NMR spectroscopy

Frans A.A. Mulder
Anthony Mittermaier
Lewis E. Kay
Research01 Nov 2001
Nature Structural Biology

Volume: 8, P: 932-935
Author Correction: Proteolytic processing induces a conformational switch required for antibacterial toxin delivery

Nicholas L. Bartelli
Victor J. Passanisi
Christopher S. Hayes
Amendments and CorrectionsOpen Access21 Oct 2022
Nature Communications

Volume: 13, P: 1
Proteolytic processing induces a conformational switch required for antibacterial toxin delivery

Contact-dependent growth inhibition (CDI) is an important mechanism of bacterial competition. Here, Bartelli et al. show that proteolytic processing of a CDI toxin induces a conformational switch required for translocation into target bacteria.

Nicholas L. Bartelli
Victor J. Passanisi
Christopher S. Hayes
ResearchOpen Access29 Aug 2022
Nature Communications

Volume: 13, P: 1-17
The solution structure and interactions of CheW from Thermotoga maritima

Ian J. Griswold
Hongjun Zhou
Frederick W. Dahlquist
Research22 Jan 2002
Nature Structural Biology

Volume: 9, P: 121-125
Slip sliding away: new insights into DNA-protein recognition

DNA-binding proteins accomplish the remarkable feat of finding their correct target sequences within a sea of genomic DNA. A new study uses NMR spectroscopy to show the mechanism by which proteins may hop between and slide along DNA as they search for their target binding sites.

Frederick W Dahlquist
News & Views01 Jul 2006
Nature Chemical Biology

Volume: 2, P: 353-354
Bigger is better: megadalton protein NMR in solution

NMR spectra recorded on the 900 kDa GroEL–GroES complex substantially raise the bar for the size of macromolecules that can be studied by NMR techniques.

Ian J. Griswold
Frederick W. Dahlquist
News & Views01 Aug 2002
Nature Structural Biology

Volume: 9, P: 567-568
Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

Guillaume Bouvignies
Pramodh Vallurupalli
Lewis E. Kay
Research21 Aug 2011
Nature

Volume: 477, P: 111-114