000 01321 a2200385 4500
005 20250511190654.0
264 0 _c19920930
008 199209s 0 0 eng d
022 _a0006-2960
024 7 _a10.1021/bi00149a004
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aLu, J
245 0 0 _aProtein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states.
_h[electronic resource]
260 _bBiochemistry
_cSep 1992
300 _a7765-72 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
650 0 4 _aBuffers
650 0 4 _aCircular Dichroism
650 0 4 _aCystamine
_xpharmacology
650 0 4 _aCysteamine
_xpharmacology
650 0 4 _aEnzyme Stability
650 0 4 _aHot Temperature
650 0 4 _aMuramidase
_xchemistry
650 0 4 _aOxidation-Reduction
650 0 4 _aProtein Conformation
650 0 4 _aProtein Denaturation
650 0 4 _aSulfhydryl Compounds
_xpharmacology
650 0 4 _aT-Phages
_xenzymology
650 0 4 _aThermodynamics
700 1 _aBaase, W A
700 1 _aMuchmore, D C
700 1 _aDahlquist, F W
773 0 _tBiochemistry
_gvol. 31
_gno. 34
_gp. 7765-72
856 4 0 _uhttps://doi.org/10.1021/bi00149a004
_zAvailable from publisher's website
999 _c1517446
_d1517446