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21 results on '"King, Jeremy D."'

9. Template-Catalyzed, Disulfide Conjugation of Monoclonal Antibodies Using a Natural Amino Acid Tag

Author

King, Jeremy D., primary, Ma, Yuelong, additional, Kuo, Yi-Chiu, additional, Bzymek, Krzysztof P., additional, Goodstein, Leah H., additional, Meyer, Kassondra, additional, Moore, Roger E., additional, Crow, Desiree, additional, Colcher, David M., additional, Singh, Gagandeep, additional, Horne, David A., additional, and Williams, John C., additional

Published
2018
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10. Mechanically interlocked functionalization of monoclonal antibodies

Author

Bzymek, Krzysztof P., primary, Puckett, James W., additional, Zer, Cindy, additional, Xie, Jun, additional, Ma, Yuelong, additional, King, Jeremy D., additional, Goodstein, Leah H., additional, Avery, Kendra N., additional, Colcher, David, additional, Singh, Gagandeep, additional, Horne, David A., additional, and Williams, John C., additional

Published
2018
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12. Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle

Author

Lu, Yue, primary, Liu, Haijun, additional, Saer, Rafael G., additional, Zhang, Hao, additional, Meyer, Christine M., additional, Li, Veronica L., additional, Shi, Liuqing, additional, King, Jeremy D., additional, Gross, Michael L., additional, and Blankenship, Robert E., additional

Published
2016
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14. Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion.

Author

Liu, Haijun, Lu, Yue, Wolf, Benjamin, Saer, Rafael, King, Jeremy D., and Blankenship, Robert E.

Abstract

Photosynthesis starts with absorption of light energy by light-harvesting antenna complexes with subsequent production of energy-rich organic compounds. However, all photosynthetic organisms face the challenge of excess photochemical conversion capacity. In cyanobacteria, non-photochemical quenching (NPQ) performed by the orange carotenoid protein (OCP) is one of the most important mechanisms to regulate the light energy captured by light-harvesting antennas. This regulation permits the cell to meet its cellular energy requirements and at the same time protects the photosynthetic apparatus under fluctuating light conditions. Several reports have revealed that thermal dissipation increases under excess copper in plants. To explore the effects and mechanisms of copper on cyanobacteria NPQ, photoactivation and relaxation of OCP in the presence of copper were examined in this communication. When OCP (OCP at orange state) is converted into OCP(OCP at red state), copper ion has no effect on the photoactivation kinetics. Relaxation of OCP to OCP, however, is largely delayed-almost completely blocked, in the presence of copper. Even the addition of the fluorescence recovery protein (FRP) cannot activate the relaxation process. Native polyacrylamide gel electrophoresis (PAGE) analysis result indicates the heterogeneous population of Cu-locked OCP. The Cu-OCP binding constant was estimated using a hyperbolic binding curve. Functional roles of copper-binding OCP in vivo are discussed. [ABSTRACT FROM AUTHOR]

Published
2018
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20. Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle

Author

Lu, Yue, Liu, Haijun, Saer, Rafael G., Zhang, Hao, Meyer, Christine M., Li, Veronica L., Shi, Liuqing, King, Jeremy D., Gross, Michael L., and Blankenship, Robert E.

Abstract

The orange carotenoid protein (OCP) and fluorescence recovery protein (FRP) are present in many cyanobacteria and regulate an essential photoprotection cycle in an antagonistic manner as a function of light intensity. We characterized the oligomerization states of OCP and FRP by using native mass spectrometry, a technique that has the capability of studying native proteins under a wide range of protein concentrations and molecular masses. We found that dimeric FRP is the predominant state at protein concentrations ranging from 3 to 180 μM and that higher-order oligomers gradually form at protein concentrations above this range. The OCP, however, demonstrates significantly different oligomerization behavior. Monomeric OCP (mOCP) dominates at low protein concentrations, with an observable population of dimeric OCP (dOCP). The ratio of dOCP to mOCP, however, increases proportionally with protein concentration. Higher-order OCP oligomers form at protein concentrations beyond 10 μM. Additionally, native mass spectrometry coupled with ion mobility allowed us to measure protein collisional cross sections and interrogate the unfolding of different FRP and OCP oligomers. We found that monomeric FRP exhibits a one-stage unfolding process, which could be correlated with its C-terminal bent crystal structure. The structural domain compositions of FRP and OCP are compared and discussed.

Published
2017
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21. Refining the Quality of Monoclonal Antibodies: Grafting Unique Peptide-Binding Site in the Fab Framework.

Author

King JD and Williams JC

Subjects
Amino Acid Sequence, Antibodies, Monoclonal chemistry, Binding Sites, Computational Biology methods, Humans, Immunoglobulin Fab Fragments chemistry, Mutation, Protein Binding immunology, Protein Engineering, Structure-Activity Relationship, Antibodies, Monoclonal genetics, Antibodies, Monoclonal immunology, Immunoglobulin Fab Fragments genetics, Immunoglobulin Fab Fragments immunology
Abstract

Monoclonal antibodies (mAbs) are a major therapeutic modality. Grafting the meditope binding site onto mAbs, also known as meditope-enabling, can extend the usefulness of mAbs by providing an additional protein-protein interaction surface without altering the stability or antigen binding. We have previously used this site for attaching dyes, cytotoxic drugs, and entire proteins. Here, we provide a simple protocol for meditope-enabling mAbs, and verifying meditope and antigen binding using flow cytometry (FACS).

Published
2019
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