TY - JOUR
T1 - Spectral studies on the denaturation of myoglobin
AU - Schechter, Alan N.
AU - Epstein, Charles J.
PY - 1968
Y1 - 1968
N2 - Absorption and fluorescence spectroscopy and optical rotation measurements have been used to follow the denaturation of sperm whale skeletal muscle and horse heart myoglobins by urea and guanidine hydrochloride. The spectral properties of the metmyoglobin forms of each of these proteins change concomitantly during denaturation, and the transitions are compatible with a one-step, cooperative denaturation process. The apomyoglobins from sperm whale and horse undergo transitions at lower concentrations of denaturants than do their respective metmyoglobins, and the data are again compatible with a one-step process. For both metmyoglobins and apomyoglobins, the protein from the sperm whale is significantly more stable than that from the horse. These results are discussed with respect to the chemical bases of the spectral properties, the location and relationship of the chromophores in the atomic model of the protein, and the forces which lead to structural stability.
AB - Absorption and fluorescence spectroscopy and optical rotation measurements have been used to follow the denaturation of sperm whale skeletal muscle and horse heart myoglobins by urea and guanidine hydrochloride. The spectral properties of the metmyoglobin forms of each of these proteins change concomitantly during denaturation, and the transitions are compatible with a one-step, cooperative denaturation process. The apomyoglobins from sperm whale and horse undergo transitions at lower concentrations of denaturants than do their respective metmyoglobins, and the data are again compatible with a one-step process. For both metmyoglobins and apomyoglobins, the protein from the sperm whale is significantly more stable than that from the horse. These results are discussed with respect to the chemical bases of the spectral properties, the location and relationship of the chromophores in the atomic model of the protein, and the forces which lead to structural stability.
UR - http://www.scopus.com/inward/record.url?scp=0014413956&partnerID=8YFLogxK
U2 - 10.1016/S0022-2836(68)80015-4
DO - 10.1016/S0022-2836(68)80015-4
M3 - Article
C2 - 5673697
AN - SCOPUS:0014413956
SN - 0022-2836
VL - 35
SP - 567
EP - 589
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -