toggle visibility
Search within Results:
Display Options:

Select All    Deselect All
List View
 |   | 
   print
  Author Title Year Publication (up) Serial Volume Pages Links
Alexander, F.; Horner, M.W.; Moss, M.S. The salivary secretion and clearance in the horse of chloral hydrate and its metabolites 1967 Biochemical pharmacology 118 16 1305-1311 details   openurl
Polverini, E.; Cugini, G.; Annoni, F.; Abbruzzetti, S.; Viappiani, C.; Gensch, T. Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red 2006 Biochemistry 3763 45 5111-5121 details   doi
Haruta, N.; Kitagawa, T. Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin 2002 Biochemistry 3785 41 6595-6604 details   openurl
Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B. Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape 2001 Biochemistry 3789 40 5137-5143 details   openurl
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. Nature of the fast and slow refolding reactions of iron(III) cytochrome c 1981 Biochemistry 3809 20 1622-1630 details   openurl
Dunn, M.F.; Branlant, G. Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation 1975 Biochemistry 3817 14 3176-3182 details   openurl
Steinhoff, H.J.; Schrader, J.; Schlitter, J. Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals 1992 Biochimica et Biophysica Acta 3800 1121 269-278 details   openurl
Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements 1989 Biochimica et Biophysica Acta 3803 996 49-56 details   openurl
Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K. Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide 1977 Biochimica et Biophysica Acta 3815 460 480-489 details   doi
Cho, K.C.; Chan, K.K. Kinetics of cold-induced denaturation of metmyoglobin 1984 Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology 3978 786 103-108 details   url
Select All    Deselect All
List View
 |   | 
   print

Save Citations: