000 | 01556 a2200421 4500 | ||
---|---|---|---|
005 | 20250515141220.0 | ||
264 | 0 | _c20081224 | |
008 | 200812s 0 0 eng d | ||
022 | _a1096-0384 | ||
024 | 7 |
_a10.1016/j.abb.2008.09.013 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aChang, Jui-Yoa | |
245 | 0 | 0 |
_aDenaturation and unfolding of human anaphylatoxin C3a: an unusually low covalent stability of its native disulfide bonds. _h[electronic resource] |
260 |
_bArchives of biochemistry and biophysics _cDec 2008 |
||
300 |
_a104-10 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 |
_aAnaphylatoxins _xchemistry |
650 | 0 | 4 | _aCircular Dichroism |
650 | 0 | 4 |
_aComplement C3a _xchemistry |
650 | 0 | 4 |
_aDisulfides _xchemistry |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Conformation |
650 | 0 | 4 |
_aPeptides _xchemistry |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Denaturation |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 | _aProtein Structure, Secondary |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aSpectrophotometry _xmethods |
700 | 1 | _aLin, Curtis C-J | |
700 | 1 | _aSalamanca, Silvia | |
700 | 1 | _aPangburn, Michael K | |
700 | 1 | _aWetsel, Rick A | |
773 | 0 |
_tArchives of biochemistry and biophysics _gvol. 480 _gno. 2 _gp. 104-10 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.abb.2008.09.013 _zAvailable from publisher's website |
999 |
_c18318901 _d18318901 |