Haopeng Li
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Lecture
Also affiliated: Zhejiang Sci-Tech University (2015–2018); North China Electric Power University (2025); Shandong University (2018–2021); Tampere University (2021); Anhui University of Science and Technology (2020–2021); China University of Mining and Technology (2019–2025); State Council of the People's Republic of China (2017); Second Affiliated Hospital of Xi'an Jiaotong University (2023); Chinese People's Armed Police Force Engineering University (2024); Hangzhou Xixi hospital (2017); Henan Polytechnic University (2024); Shandong Institute of Business and Technology (2024)
Faculty Researcher
Research Areas
Links
Biography and Research Information
OverviewAI-generated summary
Haopeng Li's research primarily investigates magnetorheological fluids and their applications, with a focus on high-temperature resistance and stability. His work includes developing novel magnetorheological fluids, such as silicone oil-based fluids with fumed silica additives, and exploring their temperature-dependent constitutive models. Li has also studied the preparation of magnetorheological fluids for high-temperature environments. His research extends to the properties and behavior of concrete under early-age loading, examining its mechanical and permeability characteristics and underlying mechanisms. Additionally, Li has investigated the combustion properties and emissions of low-grade biomass materials and briquettes. He has published 73 papers, accumulating 664 citations and an h-index of 14. Li collaborates with several researchers at the University of Arkansas at Fayetteville, including Jiali Li, Yeasin Ahmed, and Ruben Michael Ceballos.
Metrics
- h-index: 14
- Publications: 73
- Citations: 664
Selected Publications
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Sensing RNA’s Conformation with a Solid-State Nanopore Device at Various pH and Temperature (2026)Journal of the Arkansas Academy of Science OpenAlex
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BPS2025 - Sensing RNA stability by a silicon nitride nanopore device (2025)
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Dependence of protein shape and stability on electric field strength and solution environment (2024)
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Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature (2024)
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Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores (2023)
Collaboration Network
Top Collaborators
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores
- Dependence of protein shape and stability on electric field strength and solution environment
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
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