CYC1/YJR048W Literature Guide Help

Other names published for CYC1: iso-1-cytochrome c, YJR048W

CYC1 - Protein Physical Properties (203)

Results: 121 - 150 of 203 records
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ReferenceOther Genes Addressed
Moore GR, et al.  (1998) N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J 332 ( Pt 2)():439-49
Pearce DA and Sherman F  (1998) Degradation of yeast cytochromes c dependent and independent on its physiological partners. Arch Biochem Biophys 352(1):85-96
Silkstone G, et al.  (1998) Yeast iso-1-cytochrome c met80X mutants: the pKa of the spin state transition as a probe for haem pocket flexibility. Biochem Soc Trans 26(4):S348
Banci L, et al.  (1997) A molecular dynamics study in explicit water of the reduced and oxidized forms of yeast iso-1-cytochrome c--solvation and dynamic properties of the two oxidation states. Eur J Biochem 249(3):716-23
Banci L, et al.  (1997) Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c. Biochemistry 36(29):8992-9001
Fetrow JS, et al.  (1997) Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c. Protein Sci 6(1):197-210
Godbole S and Bowler BE  (1997) A histidine variant of yeast iso-1-cytochrome c that strongly affects the energetics of the denatured state. J Mol Biol 268(5):816-21
Godbole S, et al.  (1997) A lysine 73-->histidine variant of yeast iso-1-cytochrome c: evidence for a native-like intermediate in the unfolding pathway and implications for m value effects. Biochemistry 36(1):119-26
Herrmann LM and Bowler BE  (1997) Thermal denaturation of iso-1-cytochrome c variants: comparison with solvent denaturation. Protein Sci 6(3):657-65
Kotlyar AB and Borovok N  (1997) Intramolecular oxidation of cytochrome c by covalently attached sulfoaromatic molecules. Biochim Biophys Acta 1321(3):221-8
Qu K, et al.  (1997) Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102. Biochemistry 36(10):2884-97
Schroeder HR, et al.  (1997) The polarity of tyrosine 67 in yeast iso-1-cytochrome c monitored by second derivative spectroscopy. Biochem Cell Biol 75(3):191-7
Sukits SF and Satterlee JD  (1997) Sequential main-chain proton and carbon resonance assignments for wild-type yeast iso-1 ferrocytochrome c and identification of secondary structural elements. J Protein Chem 16(8):775-86
Sukits SF, et al.  (1997) Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase. Biochemistry 36(17):5251-9
Winkler JR, et al.  (1997) Effects of folding on metalloprotein active sites. Proc Natl Acad Sci U S A 94(9):4246-9
Betz SF, et al.  (1996) Unusual effects of an engineered disulfide on global and local protein stability. Biochemistry 35(23):7422-8
Doyle DF, et al.  (1996) Changing the transition state for protein (Un) folding. Biochemistry 35(23):7403-11
Lett CM, et al.  (1996) The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c. J Biol Chem 271(46):29088-93
Malatesta F, et al.  (1996) Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking. Biochem J 315 ( Pt 3)():909-16
Banci L, et al.  (1995) Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity. Biochemistry 34(36):11385-98
Banci L, et al.  (1995) pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein. Chem Biol 2(6):377-83
Herrmann L, et al.  (1995) The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: investigation of aliphatic residues. Biochemistry 34(9):3040-7
Linske-O'Connell LI, et al.  (1995) Site specific combinations of stabilizing and destabilizing amino acid replacements in yeast cytochrome c: in vivo and in vitro effects. Biochemistry 34(21):7103-12
Linske-O'Connell LI, et al.  (1995) Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochrome c: in vivo and in vitro effects. Biochemistry 34(21):7094-102
Matthis AL and Erman JE  (1995) Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters. Biochemistry 34(31):9985-90
Matthis AL, et al.  (1995) Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength. Biochemistry 34(31):9991-9
Miller MA, et al.  (1995) Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase. Biochemistry 34(37):12048-58
Pearce DA and Sherman F  (1995) Enhanced stability in vivo of a thermodynamically stable mutant form of yeast iso-1-cytochrome c. Mol Gen Genet 249(2):155-61
Pielak GJ, et al.  (1995) Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry 34(10):3268-76
Berghuis AM, et al.  (1994) The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. J Mol Biol 236(3):786-99
Results: 121 - 150 of 203 records
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