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Biochemistry|April 18, 1989
Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobinJ Ramsden, T G SpiroBiochimica Et Biophysica Acta|July 18, 1985
Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidaseG Smulevich, T G SpiroBiochemistry|January 31, 1998
Tyrosine and tryptophan structure markers in hemoglobin ultraviolet resonance Raman spectra: mode assignments via subunit-specific isotope labeling of recombinant proteinX Hu, T G SpiroBiochemistry|November 8, 1994
Modeling the hemoglobin switchpoint with cyanomet valency hybrids: Raman spectroscopic probes of tertiary and quaternary structureI Mukerji, T G SpiroBiochemistry|July 17, 1998
Structure changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopyD Wang, T G SpiroBiochemistry|April 11, 1995
Structure of a third cooperativity state of hemoglobin: ultraviolet resonance Raman spectroscopy of cyanomethemoglobin ligation microstatesV Jayaraman, T G SpiroBiochemistry|December 21, 1982
Resonance raman spectroscopic studies of axial ligation in oxyhemoglobin, oxymyoglobin, and nitrosylmyoglobinM A Walters, T G SpiroEnvironmental Science & Technology|June 9, 2011
Peer reviewed: the u.s. Dioxin inventory: are there missing sources?V M Thomas, T G SpiroBiochemistry|May 26, 1981
Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteinsW D Bowman, T G SpiroPageof 16