Conformational changes in proteins induced by low temperatures: an infrared study.
Infrared spectra of hemoglobin (met-hemoglobin) and myoglobin were recorded in the temperature range -110 degrees C to 30 degrees C. On cooling hydroalcoholic solutions of hemoglobin, the spectra indicate a conformational change (revealed by the appearance of a band at 1665 cm-1) compatible with the appearance of distortions in its alpha-helical structure. In the case of myoglobin smaller effects are observed. These conformational changes are entirely reversible and do not occur in frozen aqueous solutions.
Casal
H L
HL
Division of Chemistry, National Research Council of Canada, Ottawa.
Köhler
U
U
Mantsch
H H
HH
Goñi
F M
FM
Arrondo
J L
JL
D000818:Animals; D003080:Cold Temperature; D006454:Hemoglobins; D006801:Humans; D009211:Myoglobin; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D014907:Whales
D006454:Hemoglobins; D009211:Myoglobin