000 01488 a2200373 4500
005 20250515203418.0
264 0 _c20100312
008 201003s 0 0 eng d
022 _a1091-6490
024 7 _a10.1073/pnas.0914163107
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aBoehr, David D
245 0 0 _aMillisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands.
_h[electronic resource]
260 _bProceedings of the National Academy of Sciences of the United States of America
_cJan 2010
300 _a1373-8 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
650 0 4 _aEscherichia coli
_xenzymology
650 0 4 _aLigands
650 0 4 _aModels, Molecular
650 0 4 _aNADP
_xchemistry
650 0 4 _aNuclear Magnetic Resonance, Biomolecular
650 0 4 _aProtein Binding
650 0 4 _aProtein Structure, Tertiary
650 0 4 _aSubstrate Specificity
650 0 4 _aTetrahydrofolate Dehydrogenase
_xchemistry
650 0 4 _aTetrahydrofolates
_xgenetics
650 0 4 _aThermodynamics
650 0 4 _aTime Factors
700 1 _aMcElheny, Dan
700 1 _aDyson, H Jane
700 1 _aWright, Peter E
773 0 _tProceedings of the National Academy of Sciences of the United States of America
_gvol. 107
_gno. 4
_gp. 1373-8
856 4 0 _uhttps://doi.org/10.1073/pnas.0914163107
_zAvailable from publisher's website
999 _c19457922
_d19457922