000			01219 a2200301 4500
005			20250516154912.0
264		0	_c20131024
008			201310s 0 0 eng d
022			_a1734-154X
040			_aNLM _beng _cNLM
100	1		_aArumugam, Muthu
245	0	0	_aHeat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis. _h[electronic resource]
260			_bActa biochimica Polonica _c2013
300			_a199-207 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aElectrophoresis, Polyacrylamide Gel
650	0	4	_aHydrophobic and Hydrophilic Interactions
650	0	4	_aModels, Molecular
650	0	4	_aMycobacterium smegmatis _xenzymology
650	0	4	_aMycobacterium tuberculosis _xenzymology
650	0	4	_aNucleoside-Diphosphate Kinase _xchemistry
650	0	4	_aProtein Multimerization _xphysiology
650	0	4	_aProtein Structure, Quaternary
650	0	4	_aRecombinant Proteins _xchemistry
650	0	4	_aSodium Dodecyl Sulfate _xpharmacology
700	1		_aAjitkumar, Parthasarathi
773	0		_tActa biochimica Polonica _gvol. 60 _gno. 2 _gp. 199-207
999			_c22855288 _d22855288