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Author (down) Dyson, H.J.; Beattie, J.K. openurl 
  Title Spin state and unfolding equilibria of ferricytochrome c in acidic solutions Type Journal Article
  Year 1982 Publication The Journal of Biological Chemistry Abbreviated Journal J Biol Chem  
  Volume 257 Issue 5 Pages 2267-2273  
  Keywords Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature  
  Abstract Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions.  
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  Language English Summary Language Original Title  
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  ISSN 0021-9258 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:6277891 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3807  
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Author (down) Cho, K.C.; Chan, K.K. url  openurl
  Title Kinetics of cold-induced denaturation of metmyoglobin Type Journal Article
  Year 1984 Publication Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology Abbreviated Journal  
  Volume 786 Issue 1-2 Pages 103-108  
  Keywords Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart)  
  Abstract Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order.  
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  Notes Approved no  
  Call Number refbase @ user @ Serial 3978  
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Author (down) Bayley, P.; Martin, S.; Anson, M. openurl 
  Title Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution Type Journal Article
  Year 1975 Publication Biochemical and Biophysical Research Communications Abbreviated Journal Biochem Biophys Res Commun  
  Volume 66 Issue 1 Pages 303-308  
  Keywords *Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors  
  Abstract  
  Address  
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  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 0006-291X ISBN Medium  
  Area Expedition Conference  
  Notes PMID:1172440 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3816  
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Author (down) Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. openurl 
  Title Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump Type Journal Article
  Year 2000 Publication Biophysical Journal Abbreviated Journal Biophys J  
  Volume 78 Issue 1 Pages 405-415  
  Keywords Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence  
  Abstract Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation.  
  Address Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia  
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  Series Volume Series Issue Edition  
  ISSN 0006-3495 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:10620304 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3792  
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