The Experts below are selected from a list of 279 Experts worldwide ranked by ideXlab platform
Jose L Mascarenas - One of the best experts on this subject based on the ideXlab platform.
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the ββα fold of zinc finger proteins as a natural protecting group chemoselective synthesis of a dna binding zinc finger derivative
Chemical Communications, 2014Co-Authors: Jessica Rodriguez, Jesus Mosquera, Olalla Vazquez, Eugenio M Vazquez, Jose L MascarenasAbstract:We report the selective modification of Cysteine residues engineered in peptides that have two additional Cysteine residues as part of a Cys2His2 zinc finger motif. The chemoselective modification is achieved, thanks to the protecting effect exerted by the zinc cation upon coordination with the native Cysteines and histidines of the zinc-finger fold. The strategy allows a straightforward synthesis of DNA binding zinc finger constructs.
Liezelle C Lopez - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of metal ions on the formation of the thermus thermophilus sco mixed disulfide intermediate metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native Cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual Cysteines. Conjugation of TNB to the remaining Cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide intermediate. The Cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This Cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive Cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of metal ions on the ability to reduce and form a mixed disulfide intermediate are also probed.
Jessica Rodriguez - One of the best experts on this subject based on the ideXlab platform.
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the ββα fold of zinc finger proteins as a natural protecting group chemoselective synthesis of a dna binding zinc finger derivative
Chemical Communications, 2014Co-Authors: Jessica Rodriguez, Jesus Mosquera, Olalla Vazquez, Eugenio M Vazquez, Jose L MascarenasAbstract:We report the selective modification of Cysteine residues engineered in peptides that have two additional Cysteine residues as part of a Cys2His2 zinc finger motif. The chemoselective modification is achieved, thanks to the protecting effect exerted by the zinc cation upon coordination with the native Cysteines and histidines of the zinc-finger fold. The strategy allows a straightforward synthesis of DNA binding zinc finger constructs.
Jennifer R Mckinney - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of metal ions on the formation of the thermus thermophilus sco mixed disulfide intermediate metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native Cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual Cysteines. Conjugation of TNB to the remaining Cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide intermediate. The Cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This Cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive Cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of metal ions on the ability to reduce and form a mixed disulfide intermediate are also probed.
Nikita Mukhitov - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of metal ions on the formation of the thermus thermophilus sco mixed disulfide intermediate metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native Cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual Cysteines. Conjugation of TNB to the remaining Cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide intermediate. The Cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This Cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive Cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of metal ions on the ability to reduce and form a mixed disulfide intermediate are also probed.
