Chan‐Hwa Chung

ORCID: 0000-0003-2808-1001
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Protein Degradation and Inhibitors
  • Electrocatalysts for Energy Conversion
  • Advanced battery technologies research
  • Catalytic Processes in Materials Science
  • Supercapacitor Materials and Fabrication
  • Fuel Cells and Related Materials
  • Semiconductor Quantum Structures and Devices
  • Electrodeposition and Electroless Coatings
  • Conducting polymers and applications
  • Catalysts for Methane Reforming
  • Semiconductor materials and devices
  • Electrochemical Analysis and Applications
  • Advancements in Battery Materials
  • Advanced Photocatalysis Techniques
  • Nanoporous metals and alloys
  • Electrochemical sensors and biosensors
  • Advanced biosensing and bioanalysis techniques
  • Advanced Semiconductor Detectors and Materials
  • Multiple Myeloma Research and Treatments
  • HIV/AIDS drug development and treatment
  • Quantum Dots Synthesis And Properties
  • Glioma Diagnosis and Treatment
  • Click Chemistry and Applications
  • Gas Sensing Nanomaterials and Sensors
  • Advanced Battery Materials and Technologies

Sungkyunkwan University
2016-2025

LG Chem (South Korea)
2022

Institute of Physics, Academia Sinica
2021

Suwon Research Institute
2014-2019

Government of the Republic of Korea
2016-2019

Seoul National University
1992-2013

University of Connecticut
1992-2005

Bio-Medical Science (South Korea)
2003-2005

Electronics and Telecommunications Research Institute
2003-2004

National Sun Yat-sen University
2002

We have isolated a new type of ATP-dependent protease from Escherichia coli. It is the product heat-shock locus hslVU that encodes two proteins: HslV, 19-kDa protein similar to proteasome beta subunits, and HslU, 50-kDa related ATPase ClpX. In presence ATP, hydrolyzes rapidly fluorogenic peptide Z-Gly-Gly-Leu-AMC very slowly certain other chymotrypsin substrates. This activity increased 10-fold in E. coli expressing proteins constitutively 100-fold cells HslV HslU high copy plasmid. Although...

10.1073/pnas.93.12.5808 article EN Proceedings of the National Academy of Sciences 1996-06-11

10.1016/j.elecom.2010.01.021 article EN Electrochemistry Communications 2010-01-22

In addition to protease La (the lon gene product), Escherichia coli contains another ATP-dependent protease, Ti. This enzyme (approximately 340 kDa) is composed of two components, both which are required for proteolysis. Both have been purified homogeneity by conventional procedures using [3H]casein as the substrate. The ATP-stabilized component, A, has a subunit molecular weight 80,000 upon gel electrophoresis in presence sodium dodecyl sulfate, but it behaves dimer (140 filtration....

10.1016/s0021-9258(18)68366-8 article EN cc-by Journal of Biological Chemistry 1988-06-01

Abstract Functional groups in two‐dimensional (2D) Ti 3 C 2 T x MXene are an important factor influencing electrochemical performance many applications involving energy storage, sensors, and water purification. However, after dimethyl sulfoxide (DMSO) delamination, the effect of surface functionalities is still unclear there no systematic reports on its capacitive behavior. Experiments theoretical calculations confirm relationship between different functionalities, DMSO delamination effect,...

10.1002/cssc.201801759 article EN ChemSusChem 2018-09-04

Exploration of novel single or Z-scheme based composite photocatalysts is pursued for solar–chemical energy conversion.

10.1039/c7nr07952d article EN Nanoscale 2018-01-01

The energy requirement for protein breakdown in Escherichia coli has generally been attributed to the ATP-dependence of protease La, lon gene product. We have partially purified another ATP-dependent from lon-cells that lack La (as shown by immunoblotting). This enzyme hydrolyzes [3H]methyl-casein acid-soluble products presence ATP and Mg2+. hydrolysis appears necessary proteolytic activity. Since this is inhibited diisopropyl fluorophosphate, it be a serine protease, but also contains...

10.1073/pnas.84.16.5550 article EN Proceedings of the National Academy of Sciences 1987-08-01

Protease Ti, a new ATP-dependent protease in Escherichia coli, degrades proteins and ATP linked process, but these two hydrolytic functions are catalyzed by distinct components of the enzyme. To clarify enzyme's specificity role ATP, variety fluorogenic peptides were tested as possible substrates for Ti or its components. rapidly hydrolyzed N-succinyl(Suc)-Leu-Tyr-amidomethylcoumarin (AMC) (Km = 1.3 mM) which is not degraded La, other E. coli. also hydrolyzed, slowly, Suc-Ala-Ala-Phe-AMC...

10.1016/s0021-9258(18)94145-1 article EN cc-by Journal of Biological Chemistry 1989-02-01

Abstract Functional materials with attractive electronic and photoelectronic properties show great promise in various fields. In recent decades, tremendous research efforts have been devoted to the design of photoactive electroactive for qualitative quantitative analysis environmental pollutants. This review gives a concise overview on fundamentals progress functional material‐based electrochemical photoelectrochemical technology pollutant monitoring. The rational promoted basic signaling...

10.1002/adfm.202008227 article EN Advanced Functional Materials 2020-11-10

Abstract Electrochemical CO 2 reduction reaction (CO RR) to produce value‐added multi‐carbon chemicals has been an appealing approach achieving environmentally friendly carbon neutrality in recent years. Despite extensive research focusing on the use of high‐value like high‐energy‐density hydrocarbons, there have few reports production propane (C 3 H 8 ), which requires chain elongation and protonation. A rationally designed 0D/2D hybrid Cu O anchored‐Ti C T x MXene catalyst (Cu O/MXene) is...

10.1002/advs.202405154 article EN cc-by Advanced Science 2024-08-19

Incorporation of MOFs into COF pores (IL@MC QSSE) greatly facilitates lithium-ion transport for outstanding cycling performance Li metal batteries.

10.1039/d3ta07329g article EN Journal of Materials Chemistry A 2024-01-01

The product of the lon gene in Escherichia coli is an ATP-dependent protease, protease La, that also binds strongly to DNA. Addition double-stranded or single-stranded DNA presence ATP was found stimulate hydrolysis casein globin 2- 7-fold, depending on concentration. Native from several sources (plasmid pBR322, phage T7, calf thymus) had similar effects, but after denaturation 20-100% more effective than native form. Although poly(rA), mRNA, and various tRNAs did not proteolysis, poly(rC)...

10.1073/pnas.79.3.795 article EN Proceedings of the National Academy of Sciences 1982-02-01
Coming Soon ...