Hanbin Jeong

Vollum Institute

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Changwook Lee

Ulsan National Institute of Science and Technology

Jae Kwan Lee

Chosun University

April Goehring

Vollum Institute

Sarah Clark

Vollum Institute

Eric Gouaux

Oregon Health & Science University

Youngsoo Jun

Gwangju Institute of Science and Technology

Emad Tajkhorshid

University of Illinois Urbana-Champaign

Ali Rasouli

Moderna Therapeutics (United States)

Jumi Park

Ulsan National Institute of Science and Technology

Sepehr Dehghani‐Ghahnaviyeh

University of Illinois Urbana-Champaign

Cooperative Institutions

Ulsan National Institute of Science and Technology

Seoul National University

Government of the Republic of Korea

Gwangju Institute of Science and Technology

Korea Institute of Science and Technology

Korea University

Yonsei University

Chosun University

Daegu-Gyeongbuk Medical Innovation Foundation

Sungkyunkwan University

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Improved External Quantum Efficiency from Solution-Processed (CH₃NH₃)PbI₃ Perovskite/PC₇₁BM Planar Heterojunction for High Efficiency Hybrid Solar Cells

The Journal of Physical Chemistry C (2014)

Sanghyun Paek Nara Cho Hyeju Choi Hanbin Jeong Jin Sung Lim

Well-organized (CH3NH3)PbI3 perovskite films fabricated from various solution-processing conditions were characterized and used in hybrid solar cells with PC71BM planar heterojuncion films, exhibiting a high power-conversion efficiency of 12.2% with the better photocurrent and fill factor compared to those with PC61BM due to a better spectral response in the visible region and a better planar junction with the Ag electrode than the PC61BM.

Photocurrent

Quantum Efficiency

Perovskite solar cell

10.1021/jp508162p

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Citations (38)

Efficient Synthesis and Characterization of Solvatochromic Fluorophore

Bulletin of the Korean Chemical Society (2017)

Muhammad Adnan Hyeong Seok Kim Hanbin Jeong Haye Min Ko Sang Kook Woo

A highly efficient designing and synthesis of an aryl‐substituted carbazole‐based fluorescent material ( MeOCbzBP ) has been carried out via tandem carbon–carbon (C–C)/carbon–nitrogen (C–N) bond formation by multiple Suzuki couplings and Cadogan cyclization followed by C–N cross‐couplings. Various organic solvents have been used to investigate photophysical, solvatofluorochromism, and photoluminescence characteristics of MeOCbzBP . The MeOCbzBP showed a reasonable redshifted absorption in UV region and photoluminescence enhancements in tetrahydrofuran/water mixtures. Furthermore, we also employed various theoretical functions to optimize the molecule both in the ground and excited states. A well‐known density functional theory was employed in a solvent phase with B3LYP /6‐ 31G (d) level of theories. We believe that the MeOCbzBP will provide a better platform to investigate the novel applications in the field of medicinal chemistry and chemical biology.

Solvatochromism

Carbazole

Tetrahydrofuran

10.1002/bkcs.11219

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Citations (49)

Amino acids derived nitrogen-doped carbon materials for electrochemical capacitive energy storage

Materials Letters (2015)

Hanbin Jeong Hwa Jung Kim Yangjin Lee Jun Yeon Hwang Ok‐Kyung Park

Carbon fibers

Thermal Stability

10.1016/j.matlet.2015.01.067

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Citations (20)

High-modulus and strength carbon nanotube fibers using molecular cross-linking

Carbon (2017)

Ok‐Kyung Park Hoikil Choi Hanbin Jeong Yeonsu Jung Jaesang Yu

10.1016/j.carbon.2017.03.079

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Citations (96)

Structure of C. elegans TMC-1 complex illuminates auditory mechanosensory transduction

Zenodo (CERN European Organization for Nuclear Research) (2022)

Hanbin Jeong Sarah Clark April Goehring Sepehr Deghani-Ghahnaviyeh Ali Rasouli

Transduction (biophysics)

Auditory pathways

10.5281/zenodo.6762366

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Citations (0)

The structure of the Caenorhabditis elegans TMC-2 complex suggests roles of lipid-mediated subunit contacts in mechanosensory transduction

Proceedings of the National Academy of Sciences (2024)

Sarah Clark Hanbin Jeong Richard Posert April Goehring Eric Gouaux

Mechanotransduction is the process by which a mechanical force, such as touch, is converted into an electrical signal. Transmembrane channel-like (TMC) proteins are an evolutionarily conserved family of membrane proteins whose function has been linked to a variety of mechanosensory processes, including hearing and balance sensation in vertebrates and locomotion in Drosophila . TMC1 and TMC2 are components of ion channel complexes, but the molecular features that tune these complexes to diverse mechanical stimuli are unknown. Caenorhabditis elegans express two TMC homologs, TMC-1 and TMC-2, both of which are the likely pore-forming subunits of mechanosensitive ion channels but differ in their expression pattern and functional role in the worm. Here, we present the single-particle cryo-electron microscopy structure of the native TMC-2 complex isolated from C. elegans . The complex is composed of two copies of the pore-forming TMC-2 subunit, the calcium and integrin binding protein CALM-1 and the transmembrane inner ear protein TMIE. Comparison of the TMC-2 complex to the recently published cryo-EM structure of the C. elegans TMC-1 complex highlights conserved protein–lipid interactions, as well as a π-helical structural motif in the pore-forming helices, that together suggest a mechanism for TMC-mediated mechanosensory transduction.

Mechanotransduction

Structural motif

10.1073/pnas.2314096121

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Citations (11)

Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex

EMBO Reports (2016)

Hanbin Jeong Jumi Park Changwook Lee

10.15252/embr.201642706

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Citations (73)

Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L

Acta Crystallographica Section F Structural Biology Communications (2014)

Hanbin Jeong Hakbong Lee Changwook Lee

Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase Hrd1, plays an important role in selecting and transporting ERAD substrates for degradation in the endoplasmic reticulum. In this study, the purification, crystallization and preliminary X-ray diffraction analysis of recombinant mouse SEL1L (residues 348-533) are reported. The crystals were obtained by the hanging-drop vapour-diffusion method at pH 8.5 and 277 K using 30% 2-propanol as a precipitant. Optimized crystals diffracted to 3.3 Å resolution at a synchrotron-radiation source. Preliminary X-ray diffraction analysis revealed that the crystals belonged to space group P21 and contained four molecules per asymmetric unit, with a solvent content of 44%.

10.1107/s2053230x14023115

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Citations (1)

Highly Efficient, Reproducible, Uniform (CH₃NH₃)PbI₃ Layer by Processing Additive Dripping for Solution‐Processed Planar Heterojunction Perovskite Solar Cells

Chemistry - An Asian Journal (2016)

Hansol Kim Hanbin Jeong Jae Kwan Lee

A processing additive dripping (PAD) approach to forming highly efficient (CH3 NH3 )PbI3 (MAPbI3 ) perovskite layers was investigated. A MAPbI3 (CB/DIO) perovskite film fabricated by this approach, which included briefly dripping chlorobenzene incorporating a small amount of diiodooctane (DIO) during casting of a MAPbI3 perovskite precursor dissolved in dimethylformamide, exhibited superior smooth, uniform morphologies with high crystallinity and large grains and revealed completely homogeneous surface coverage. The surface coverage and morphology of the substrate significantly affected the photovoltaic performance of planar heterojunction (PHJ) perovskite solar cells (PrSCs), resulting in a power conversion efficiency of 11.45 % with high open-circuit voltage of 0.91 V and the highest fill factor of 80.87 %. Moreover, the PAD approach could effectively provide efficient MAPbI3 (CB/DIO) perovskite layers for highly efficient, reproducible, uniform PHJ PrSC devices without performance loss or variation even over larger active areas.

Chlorobenzene

10.1002/asia.201600722

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Citations (6)

Structure of C. elegans TMC-1 complex illuminates auditory mechanosensory transduction

Research Square (Research Square) (2022)

Eric Gouaux Sarah J. Clark Hanbin Jeong April Goehring Sepehr Dehghani‐Ghahnaviyeh

Abstract The initial step in the sensory transduction pathway underpinning hearing and balance in mammals involves the conversion of force into the gating of a mechanosensory transduction (MT) channel. Despite the profound socioeconomic impacts of hearing disorders and the fundamental biological significance of understanding MT, the composition, structure and mechanism of the MT complex has remained elusive. Here we report the single particle cryo-EM structure of the native MT TMC-1 complex isolated from C. elegans. The 2-fold symmetric complex is composed of 2 copies each of the pore-forming TMC-1 subunit, the calcium-binding protein CALM-1 and the transmembrane inner ear protein TMIE. CALM-1 makes extensive contacts with the cytoplasmic face of the TMC-1 subunits while the single-pass TMIE subunits reside on the periphery of the complex, poised like the handles of an accordion. A subset of particles in addition harbors a single arrestin-like protein, ARRD-6, bound to a CALM-1 domain. Single-particle reconstructions and molecular dynamics simulations show how the MT complex deforms the membrane bilayer and suggest crucial roles for lipid-protein interactions in the mechanism by which mechanical force is transduced to ion channel gating.

Transduction (biophysics)

10.21203/rs.3.rs-1623715/v1

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Citations (2)