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Journal of Inorganic Biochemistry|August 15, 1993
Dramatic stabilization of ferricytochrome c upon reductionS Hilgen-Willis, E F Bowden, G J Pielak
Protein Expression and Purification|July 5, 2001
Characterization of horse cytochrome c expressed in Escherichia coliC N Patel, M C Lind, G J Pielak
Biochemistry|July 16, 1991
Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiaeY Gao, J Boyd, G J Pielak, et al.
European Journal of Biochemistry|February 15, 1992
Electron-proton coupling in cytochrome c studied using protein variantsY Gao, G McLendon, G J Pielak, et al.
Biochemistry|July 31, 1990
Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome cY Gao, J Boyd, R J Williams, et al.
Biotechniques|May 1, 1988
A rapid droplet method for Sanger dideoxy sequencingS S Ner, D B Goodin, G J Pielak, et al.
Biochemistry|October 4, 1988
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this positionG V Louie, G J Pielak, M Smith, et al.
European Journal of Biochemistry|October 15, 1988
Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c familyG J Pielak, J Boyd, G R Moore, et al.
Protein Engineering|February 1, 1987
Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant proteinR L Cutler, G J Pielak, A G Mauk, et al.
Biochemistry|February 19, 1991
Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shiftsY A Gao, J Boyd, G J Pielak, et al.
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