title: Conformational changes in proteins induced by low temperatures: an infrared study.
abstract: 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.
authors.affiliation: Division of Chemistry, National Research Council of Canada, Ottawa.
authors.forename: H L
authors.initials: HL
authors.lastname: Casal
authors.forename: U
authors.initials: U
authors.lastname: Köhler
authors.forename: H H
authors.initials: HH
authors.lastname: Mantsch
authors.forename: F M
authors.initials: FM
authors.lastname: Goñi
authors.forename: J L
authors.initials: JL
authors.lastname: Arrondo
mesh_terms: D000818:Animals; D003080:Cold Temperature; D006454:Hemoglobins; D006801:Humans; D009211:Myoglobin; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D014907:Whales
chemical_list: D006454:Hemoglobins; D009211:Myoglobin