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Biochemistry|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 SpiroAccounts of Chemical Research|March 27, 2001
Is the CO adduct of myoglobin bent, and does it matter?T G Spiro, P M KozlowskiBiochemistry|April 9, 1985
Ultraviolet resonance Raman spectra of insulin and alpha-lactalbumin with 218- and 200-nm laser excitationR P Rava, T G SpiroScience (New York, N.Y.)|September 16, 1994
Nanosecond dynamics of the R-->T transition in hemoglobin: ultraviolet Raman studiesK R Rodgers, T G SpiroBiochimica Et Biophysica Acta|September 5, 1986
Tyrosine and tryptophan modification monitored by ultraviolet resonance Raman spectroscopyD S Caswell, T G SpiroBiochemistry|April 21, 1987
Secondary structure determination in proteins from deep (192-223-nm) ultraviolet Raman spectroscopyR A Copeland, T G SpiroPageof 10