| 000 | 01852 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250517110157.0 | ||
| 264 | 0 | _c20180126 | |
| 008 | 201801s 0 0 eng d | ||
| 022 | _a1091-6490 | ||
| 024 | 7 |
_a10.1073/pnas.1604748113 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aFalk, Bradley T | |
| 245 | 0 | 0 |
_aChemical shift imprint of intersubunit communication in a symmetric homodimer. _h[electronic resource] |
| 260 |
_bProceedings of the National Academy of Sciences of the United States of America _c08 2016 |
||
| 300 |
_a9533-8 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, N.I.H., Extramural | ||
| 650 | 0 | 4 | _aAllosteric Regulation |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 |
_aDeoxyuracil Nucleotides _xchemistry |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 |
_aEscherichia coli Proteins _xchemistry |
| 650 | 0 | 4 | _aGene Expression |
| 650 | 0 | 4 |
_aGenetic Vectors _xchemistry |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 | _aNitrogen Isotopes |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation, alpha-Helical |
| 650 | 0 | 4 | _aProtein Conformation, beta-Strand |
| 650 | 0 | 4 | _aProtein Interaction Domains and Motifs |
| 650 | 0 | 4 | _aProtein Multimerization |
| 650 | 0 | 4 |
_aProtein Subunits _xchemistry |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSignal Transduction |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 | _aThermodynamics |
| 650 | 0 | 4 |
_aThymidylate Synthase _xchemistry |
| 700 | 1 | _aSapienza, Paul J | |
| 700 | 1 | _aLee, Andrew L | |
| 773 | 0 |
_tProceedings of the National Academy of Sciences of the United States of America _gvol. 113 _gno. 34 _gp. 9533-8 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1073/pnas.1604748113 _zAvailable from publisher's website |
| 999 |
_c26273593 _d26273593 |
||