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Professor Mikko Haataja is a distinguished faculty member in the Department of Mechanical and Aerospace Engineering at Princeton University's School of Engineering and Applied Science. Holding a Ph.D. from McGill University (2003), he leads the Haataja Research Group focused on theoretical and computational approaches to materials science and physical biology. His office is located in D404C Engineering Quadrangle, and he serves as an advisor to numerous graduate students working at the intersection of physics, materials science, and biology. Professor Haataja's research spans multiple domains including theoretical and computational materials science, physics of materials, and physical biology. His work examines microstructure formation during solid-solid phase transformations and solidification, growth of electrodeposited thin films and quantum heterostructures, dynamics of driven interfaces with mobile impurities, recrystallization kinetics, cell signaling mechanisms, and the regulation & self-organization of 'lipid rafts' in plasma membranes. His group has pioneered concepts in 'dynamically programmable electromechanical 2D materials' and investigates phase separation phenomena in biological systems. His publication record demonstrates significant contributions across several key areas: intracellular phase transitions and biomolecular condensates, 2D transition metal dichalcogenide materials, lipid bilayer membrane physics, solid oxide fuel cells and batteries, and organic semiconductor thin films. His most recent work focuses on amyloid-like fibril formation, liquid-liquid phase separation in biological contexts, and defect engineering in 2D materials, reflecting his interdisciplinary approach that bridges physics, materials science, and biology. Professor Haataja actively mentors graduate students and postdoctoral researchers, with numerous co-authored publications indicating strong advising relationships. His research program encompasses multiple funded projects investigating materials for energy conversion and storage, intracellular organization mechanisms, and novel 2D material systems. The Haataja Group maintains strong collaborations with other Princeton researchers and external institutions, particularly in the fields of biophysics and advanced materials. The Haataja Group operates as a dynamic research laboratory employing computational modeling and theoretical approaches to address fundamental questions in materials science and biophysics. Their work spans from atomic-scale simulations to continuum modeling, with particular emphasis on phase-field crystal models, membrane biophysics, and 2D material systems. The group maintains specialized computational infrastructure for multiscale modeling and collaborates extensively with experimental groups to validate theoretical predictions.

• Theoretical and computational materials science
• Physics of materials
• Physical biology
• +13 more

David S. Eisenberg is a Professor of Chemistry and Biochemistry and Biological Chemistry at the University of California, Los Angeles, where he also serves as Director of the UCLA-DOE Institute for Genomics and Proteomics and as an HHMI Investigator. His research focuses on protein interactions, particularly the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. Dr. Eisenberg earned his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University on a Rhodes Scholarship. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. He joined the UCLA faculty after his postdoctoral studies. Dr. Eisenberg and his research group focus on protein interactions in amyloid and prion diseases. These diseases involve protein aggregation where normal functional proteins convert to abnormal aggregated forms. Systemic amyloid diseases like dialysis-related amyloidosis result from fiber accumulation until organ failure, while neurodegenerative diseases like Alzheimer's, Parkinson's, ALS, and prion conditions appear to be caused by smaller oligomers. In 2005, his team determined the atomic-level structure for the amyloid fiber spine, revealing a 'steric zipper' of two parallel beta sheets packed across a dry interface. Since then, they've determined approximately 90 amyloid spines from 15 disease-related proteins. In 2010, they identified the structure of a toxic amyloid-related oligomer consisting of six anti-parallel beta strands forming a cylindrical barrel. His recent publications demonstrate continued innovation in amyloid research, with focus areas including structural prediction of amyloid formation, mechanisms of tau fibril disassembly in Alzheimer's disease, cryo-EM analysis of amyloid polymorphism, and structure-based design of inhibitors for amyloid toxicity. His work integrates computational, structural, and biochemical approaches to understand protein aggregation across multiple disease contexts. Dr. Eisenberg has received numerous prestigious awards and honors: National Academy of Sciences Member American Philosophical Society Member Institute of Medicine Member Howard Hughes Medical Institute Investigator Biophysical Society Emily M. Gray Award Harvard Westheimer Medal UCLA Seaborg Medal Technion - Israel Institute of Technology Harvey Prize in Human Health As Director of the UCLA-DOE Institute for Genomics and Proteomics and an HHMI Investigator, Dr. Eisenberg leads significant research initiatives in protein structure and aggregation. His laboratory combines X-ray crystallography, bioinformatics, and biochemical techniques to investigate protein interactions, with particular emphasis on amyloid-forming proteins and their role in disease. The Eisenberg Lab, located in Boyer Hall at UCLA, maintains an active research program investigating the structural basis of protein aggregation. The lab continues to build on its landmark discoveries of amyloid structures while exploring new frontiers in understanding protein misfolding diseases and developing potential therapeutic interventions.

• Protein Aggregation
• Amyloid Structures
• Prion Diseases
• +5 more

Andrew D. White is an Associate Professor of Chemical Engineering at the Hajim School of Engineering & Applied Sciences, University of Rochester. He holds a PhD from the University of Washington (2013). His research focuses on automating scientific discovery through AI, particularly leveraging large language models (LLMs) and deep learning techniques in chemistry. His lab develops agents that integrate literature analysis, hypothesis generation, and experimental design to advance fields like molecular dynamics and drug discovery. Education: PhD in Chemical Engineering, University of Washington, 2013 BS/MS (not explicitly stated in text, inferred from career timeline) Research Interests: Large language models for scientific automation Deep learning applications in chemistry and materials science Molecular dynamics simulations Scientific agents and autonomous systems Publications: His work includes groundbreaking studies on closed-loop AI systems for chemistry, federated learning in molecular property prediction, and multi-agent systems for drug discovery. Recent highlights include the Robin system and ChemCrow tools. Awards: Recipient of the NSF Career Award (2018), NIH Outstanding Investigator Award (2020), and the Curtis Teaching Award (2019). He also advises biotech companies and serves on the National Academy of Sciences' Chemical Sciences Roundtable. Grants & Funding: Supported by DOE, NSF (multiple grants including CBET-1751471), NIH (R35GM137966), and LLNL projects. Collaborates with institutions like Argonne National Lab and Qubit Pharmaceuticals. Labs & Teams: Leads the White Lab at Rochester and co-founded FutureHouse, a nonprofit advancing AI-driven scientific discovery. Supervises a multidisciplinary team of PhD students and postdocs in computational chemistry, AI, and biophysics.

• Large language models
• Deep learning in chemistry
• Molecular dynamics
• +5 more

Masato Kato serves as Professor in the Department of Biochemistry at the University of Texas Southwestern Medical Center since 2020 and concurrently as Team Leader at Japan's National Institutes for Quantum and Radiological Science and Technology. His academic trajectory includes progressive appointments from Assistant Professor (2004-2014) to Associate Professor (2014-2020) at UT Southwestern, with prior postdoctoral training at Harvard Medical School and Nara Institute of Science and Technology. 2020-present: Professor, Department of Biochemistry, UT Southwestern 2020-present: Team Leader, National Institutes for Quantum and Radiological Science and Technology, Japan 2014-2020: Associate Professor, Department of Biochemistry, UT Southwestern 2010-2014: Assistant Professor, Department of Biochemistry and Internal Medicine, UT Southwestern 2004-2010: Assistant Professor, Department of Internal Medicine, UT Southwestern 1999-2004: Postdoctoral Fellow, Ellenberger Lab, Harvard Medical School 1998-1999: Postdoctoral Fellow, Hakoshima Lab, Nara Institute of Science and Technology Dr. Kato's research pioneers the biophysical characterization of protein phase separation, particularly focusing on low-complexity domains (LCDs) in neurodegenerative disease contexts. His work establishes fundamental mechanisms of biomolecular condensate formation, including hydrogel polymerization, liquid-solid transitions, and mutation-induced dysregulation in ALS/FTD. Key contributions demonstrate how C9orf72-encoded poly-dipeptides disrupt nucleocytoplasmic transport and how redox states regulate Ataxin-2 phase behavior, bridging structural biochemistry with pathological mechanisms. Analysis of his 22 publications reveals a cohesive research program centered on LCD-driven phase transitions. The most recent 15 articles (2012-2019) systematically investigate pathological aggregation in neurodegeneration, structural basis of condensate formation, and regulatory mechanisms like phosphorylation and oxidation. This body of work establishes LCDs as central players in both physiological RNA granule assembly and disease-associated solidification, with strong emphasis on C9orf72-related ALS/FTD mechanisms. Dr. Kato maintains active leadership within the McKnight Laboratory at UT Southwestern, where his team employs integrated approaches spanning structural biology, cell biology, and biophysics to dissect phase separation mechanisms. His collaborative network includes prominent neuroscience and biochemistry groups, with co-authorship on key studies in Cell, Science, and PNAS.

• Protein Phase Separation
• Low-Complexity Domains
• RNA Granule Biogenesis
• +3 more

Anthony D. Wagner is the Lucie Stern Professor in the Department of Psychology at Stanford University and Deputy Director of the Wu Tsai Neurosciences Institute. He holds affiliations with Stanford's Center for Cognitive and Neurobiological Imaging, Symbolic Systems Program, Human Biology Program, and Stanford Center on Longevity. His PhD (1997) is from Stanford University in Psychology. Research focuses on the neurobiology of learning, memory, and executive function across ages, with translational studies on aging, Alzheimer’s disease, multitasking, and neuroscience applications in law. Key themes include biomarker development for neurodegeneration, cognitive resilience, and the impact of attention on memory. Labs/teams include collaborations at the Wu Tsai Institute and neuroimaging centers. Recent work emphasizes tau PET imaging, proteomics of aging, and fluid biomarkers for Alzheimer’s prediction. He also explores societal impacts of neurotechnology and media on cognition.

• Neuroscience
• Aging
• Memory
• +6 more

Celeste Sagui is a Professor in the Department of Physics at North Carolina State University (NC State), affiliated with the College of Sciences. She holds additional roles as a faculty affiliate in Genomics Sciences at NC State and is a member of the Center for High Performance Simulation. Her research focuses on computational biophysics, biomolecular simulations, and free energy methods applied to nucleic acid structures, protein dynamics, and nanotechnology systems. She has contributed to the AMBER simulation package development, co-authoring versions from 10 to 14. Education: Doctorate in Physics, University of Toronto (1995) Licentiate degree, National University of San Luis, Argentina Research Interests: Sagui’s work explores DNA/RNA structure and phase transitions, electrostatic interactions, and methodologies for large-scale molecular simulations. Recent studies include nucleic acid hairpin instabilities linked to neurodegenerative diseases, polyglutamine aggregation mechanisms, and novel DNA motifs like the eGZ structure in Z-DNA. She employs quantum chemistry, density functional theory, and phase-field models to investigate systems ranging from biomolecules to nanomaterials. Publications: Her recent work emphasizes nucleic acid dynamics, free energy landscapes, and computational methods for studying diseases such as Friedreich’s ataxia and polyglutamine disorders. Key contributions include advancements in laser-driven simulations and infrared spectroscopy analysis of protein structures. Labs/Teams: Active in the Center for High Performance Simulation, focusing on high-throughput computational modeling and collaborative software development for biomolecular research.

• Computational Biophysics
• Biomolecular Simulations
• Free Energy Methods
• +5 more

James C. Gumbart is an Adjunct Professor in the School of Physics at Georgia Institute of Technology, with additional affiliation to the School of Chemistry and the Institute for Bioengineering and Bioscience . His research leverages molecular dynamics simulations to decode the atomic-level mechanisms of bacterial proteins and cellular structures. B.S., Physics and Mathematics, Western Illinois University, 2003 Ph.D., Physics, University of Illinois at Urbana Champaign, 2009 Dr. Gumbart's work bridges computational biophysics and biochemistry to understand: Mechanisms of bacterial membrane protein insertion and nutrient import Structural dynamics of cell wall mechanics SARS-CoV-2 spike protein interactions with ACE2 Free-energy calculations for protein-ligand binding Applications of machine learning in biomolecular simulations His publications reflect trends in membrane protein biophysics , viral dynamics , and computational drug design , with a strong emphasis on interdisciplinary techniques. Awards include multiple fellowships and grants from NSF , DOE , and NIAID . He has mentored numerous PhD students, including Zijian Zhang , David Ryoo , and Andrew Pang , whose work has advanced understanding of bacterial systems and viral proteins. The Gumbart Lab integrates high-powered supercomputing and advanced software to model biomolecular processes, fostering collaborations with institutions like the National Institutes of Health and Argonne National Laboratory .

• Computational Biochemistry and Biophysics
• Membrane proteins
• Free-energy calculations
• +7 more

Professor Christopher Roland is a faculty member in the Department of Physics at North Carolina State University, part of the College of Sciences. He holds the rank of Professor since 2002, joining the university in 1993 after completing his PhD in Physics at McGill University, Canada, and postdoctoral work at the University of Toronto and AT&T Bell Laboratories. His research focuses on theoretical condensed matter physics and biophysics, particularly investigating nucleic acid structures (DNA and RNA) associated with neurodegenerative and neuromuscular disorders like Trinucleotide Repeat Expansion Diseases (TREDs). Key areas include DNA/RNA hairpin dynamics, free energy calculations, and molecular mechanisms underlying genetic mutations. Recent publications emphasize structural and computational studies of nucleic acid conformations, such as Z-DNA motifs, triplex formations, and disease-linked repeat sequences. His work bridges quantum transport simulations, biomolecular modeling, and disease prediction. No scientific awards are explicitly listed in the provided materials. His research is supported by grants from NC State University and collaborations within the Department of Physics. Laboratory and team details are not specified, though his work aligns with computational biophysics and condensed matter research groups at NC State.

• Theoretical Condensed Matter Physics
• Biophysics
• DNA/RNA Structures
• +3 more

Katherine J. Franz is a Professor of Chemistry at Duke University, affiliated with the Trinity College of Arts & Sciences and the Duke Cancer Institute. She holds a Ph.D. from MIT (2000) and a B.A. from Wellesley College (1995). Her research focuses on bioinorganic chemistry, particularly metal ion coordination in biological systems, with applications in antimicrobial therapies, cancer metallomics, and neurodegenerative diseases. Key projects include developing prochelators targeting fungal and bacterial pathogens, studying copper's role in antifungal drug efficacy, and designing light-activated metal complexes for controlled drug release. Dr. Franz has received numerous awards including the Camille Dreyfus Teacher-Scholar Award (2009), Sloan Research Fellowship (2008), and the NSF CAREER Award (2005). She leads a lab with 6 current students/mentees and has secured grants from NIH, NSF, and the US-Israel Binational Science Foundation. Her lab's work spans from fundamental metalloprotein studies to translational drug development, emphasizing interdisciplinary approaches in chemistry and biology. Education: Ph.D. in Chemistry, MIT, 2000 B.A. in Chemistry, Wellesley College, 1995 Research Interests: Metal homeostasis in pathogens, copper's role in antifungal resistance, prodrug design for targeted therapy, and mechanistic studies of metalloproteins. Grants: Tri-Institutional Molecular Mycology Training Program (NIH, 2024–2029) Duke PREP Biomedical Sciences Program (NIGMS, 2022–2027) Copper-Mucin Interaction Study (BSF, 2022–2026) Her lab's publications (n=15+ since 2020) highlight breakthroughs in prodrug selectivity, copper-induced protein toxicity, and histatin antifungal mechanisms. The Franz Lab actively collaborates with clinicians and computational scientists to advance therapeutic strategies addressing unmet medical needs in infectious diseases and cancer.

• Bioinorganic Chemistry
• Metal Homeostasis
• Antimicrobial Agents
• +4 more

James Shorter is a Professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania. He is affiliated with multiple prestigious institutes, including the Institute on Aging (IOA), the Institute for Translational Medicine and Therapeutics (ITMAT), the Penn Center for AIDS Research (CFAR), the Chemistry-Biology Interface (CBI), and the Penn Institute for RNA Innovation. He mentors several training programs such as the Penn Summer Undergraduate Internship Program (SUIP), PennPREP, and the Translational Research Immersion Program (TRIP), and serves as a Primary Trainer at the Center for Neurodegenerative Research (CNDR). Ph.D. in Cell Biology, University of London, 2000 M.A. in Biology, University of Oxford, 1995 Dr. Shorter’s research focuses on protein homeostasis, particularly the mechanisms of protein disaggregation and the role of prion-like domains in neurodegenerative diseases such as ALS, Alzheimer’s, Parkinson’s, and frontotemporal lobar degeneration. His lab investigates the Hsp104 disaggregase from yeast and has engineered variants to combat human proteinopathies. They also identified the mammalian disaggregase system (Hsp110/Hsp70/Hsp40) and explore how small molecules and nuclear import receptors can reverse pathological phase transitions of RNA-binding proteins like TDP-43 and FUS. His work bridges structural biology, genetics, and translational neuroscience. His recent publications highlight trends in targeting TDP-43 and FUS proteinopathies, engineering Hsp104 for selective detoxification, understanding mitochondrial disaggregases like Skd3, and modulating phase transitions with nuclear import receptors. His research spans from fundamental mechanisms of protein folding to therapeutic development for neurodegenerative diseases. Faculty Member, Institute on Aging (IOA) Faculty Member, Institute for Translational Medicine and Therapeutics (ITMAT) Mentor, Penn Summer Undergraduate Internship Program (SUIP) Primary Trainer, Center for Neurodegenerative Research (CNDR) Faculty Member, Penn Center for AIDS Research (CFAR) Member, Penn Institute for RNA Innovation Mentor, Translational Research Immersion Program (TRIP) Dr. Shorter advises numerous graduate students and postdoctoral researchers through the Biochemistry and Molecular Biophysics, Pharmacology, Neuroscience, and Cell and Molecular Biology graduate groups. His lab receives funding from NIH and other sources to support research on protein disaggregation, phase separation, and neurodegenerative disease mechanisms. He has trained many scientists now active in academia and biotech. His lab, located in Stellar-Chance Laboratories, operates at the intersection of biochemistry, cell biology, and translational medicine, with active projects on Hsp104 engineering, mitochondrial proteostasis, and the role of RNA-binding proteins in disease. The lab collaborates widely across Penn and with international partners to advance understanding and treatment of protein misfolding disorders.

• Protein Folding and Proteostasis
• Neurodegenerative Diseases
• Prion and Amyloid Biology
• +7 more

Hideyuki Takahashi is an Associate Research Scientist in the Department of Neuroscience at Yale University School of Medicine. He holds a PhD from Waseda University (2005) and has established himself as a prominent researcher in neurodegenerative diseases, particularly focusing on lysosomal biology and protein aggregation mechanisms. Dr. Takahashi's research primarily investigates the role of progranulin, TMEM106B, and other molecular players in neurodegenerative conditions including Alzheimer's disease, frontotemporal dementia, and tauopathies. His work spans multiple approaches from molecular and cellular neuroscience to animal models of disease. His recent publications demonstrate a strong focus on lysosomal dysfunction in neurodegeneration, with particular attention to how TMEM106B interacts with other proteins to influence disease progression. The research trends show increasing emphasis on therapeutic interventions targeting specific molecular pathways involved in protein aggregation and synaptic loss. ORCID: 0009-0004-4969-977X Dr. Takahashi maintains active collaborations with several leading researchers at Yale, most notably with Stephen Strittmatter (with whom he has 16 common publications), as well as Anita Huttner, Anthony Koleske, and Le Zhang. His research program appears well-integrated within Yale's neuroscience community, contributing significantly to our understanding of neurodegenerative disease mechanisms.

• Neuroscience
• Neurodegenerative Diseases
• Alzheimer's Disease
• +3 more

Mohtadin Hashemi is an Assistant Professor in the Department of Physics at Auburn University. His research focuses on single-molecule biophysics, studying protein-DNA interactions, membrane dynamics, and amyloid aggregation. He holds a Ph.D. in Molecular Biophysics from the University of Nebraska Medical Center (2018) and completed postdoctoral work there before joining Auburn in 2023. Education: Ph.D. (2018), M.Sc. (2013), B.Sc. (2012) in Nanotechnology and Molecular Biophysics. Affiliations: Auburn University (2023–present), University of Nebraska Medical Center (2018–2023). His research integrates biology, chemistry, and physics to elucidate molecular mechanisms of life. Key interests include single-molecule techniques, nanotechnology, and interdisciplinary collaborations. Notable awards include the 2021 European BioAFM Grand Prize and UNMC Fellowships (2017, 2016). Publications span amyloid beta interactions, lipid bilayer dynamics, and DNA-protein complexes. His lab actively mentors students and postdocs, with recent advisees including Gabriel Cathoud, Parker Ensminger, and Josiah Simes.

• Biophysics
• Single-Molecule Biophysics
• Protein-DNA Interactions
• +3 more

Anna G Orr serves as Nan and Stephen Swid Assistant Professor of Frontotemporal Dementia Research and Assistant Professor of Neuroscience at Weill Cornell Medical College's Brain and Mind Research Institute since 2016, leading pioneering research on astrocyte biology in dementia pathogenesis. Her educational background includes: Ph.D. from Emory University (2008) B.S. from Allegheny College (2002) Dr. Orr's research program centers on astrocytic-neuronal interactions , mitochondrial signaling , and neuroimmune mechanisms through three interconnected pathways: neuroimmune , oxidative , and G protein-coupled signaling . Her lab investigates how these mechanisms influence neuroinflammation, protein aggregation, synaptic function, and behavioral outcomes in dementia, with parallel therapeutic discovery efforts targeting astrocytic pathways for novel dementia treatments. Analysis of her 15 most recent publications (2025-2010) reveals escalating focus on astrocyte-specific dementia mechanisms , particularly mitochondrial ROS signaling, sex-dimorphic memory effects, TDP-43 pathology interactions with antiviral pathways, and lipid dysregulation in neurodegeneration. Her work consistently bridges molecular discoveries with therapeutic applications, demonstrating increasing NIH funding support for translational approaches. Key scientific recognitions include: NIH K99/R00 Pathway to Independence Award (2017) Leon Levy Fellowship in Neuroscience (2021) Nan and Stephen Swid Endowed Professorship (2021) Outstanding Neuroscience Teaching Award (2021) Dr. Orr actively mentors eight trainees across career stages, including Ph.D. candidates Evelyn Hardin and Constance Zhou, while securing major NIH grants as Principal Investigator for projects like Uncovering Dementia-Related Lipid Alterations in Astrocytes (NIA 2024-2026) and Mitochondrial Complex III Free Radicals in Dementia Pathology (NIA 2020-2026), alongside collaborative awards from the Alzheimer's Association. Her Orr Lab maintains a dual focus on mechanistic astrocyte biology and therapeutic translation, with current projects examining astrocytic TDP-43 dysregulation, mitochondrial complex III signaling, and sex-specific memory mechanisms using advanced in vivo techniques and disease models.

• Neuroscience
• Neurodegenerative Diseases
• Astrocyte Biology
• +5 more

Bradley Nilsson is a Professor of Chemistry at the University of Rochester, Department of Chemistry. He leads the Nilsson Group, focusing on peptide self-assembly, amyloid structures, and their applications in biomedicine and materials science. His work bridges organic, biological, and materials chemistry, with notable contributions to amyloid-inspired hydrogels and HIV transmission mechanisms. He received the 2016 Goergen Award for Excellence in Teaching and the 2012 NSF CAREER Award. Education: PhD in Organic Chemistry (2003, University of Wisconsin-Madison), postdoctoral research at UC Irvine. He joined Rochester in 2006. Research interests include molecular recognition in amyloid peptides, SEVI fibrils' role in HIV transmission, and hydrogel development for tissue engineering. His lab has pioneered studies on stimulus-responsive self-assembly and co-assembly of peptides. Key achievements include the reductive trigger for peptide hydrogelation (JACS 2010), and NIH-funded work on anti-HIV microbicides. Current projects explore amyloid-β oligomer toxicity, SEVI mechanisms, and functional biomaterials from simple amino acid derivatives. Lab members include graduate students Elena Quigley, Melissa Jagrosse, Francine Yanchik, Hannah Distaffen, and Chris Jones. The lab collaborates on interdisciplinary projects funded through NIH and NSF grants.

• Peptide self-assembly
• Amyloid structures
• HIV transmission mechanisms
• +5 more

John Straub is a Professor of Chemistry at Boston University, affiliated with the Chemistry Department. His research focuses on theoretical and computational studies of protein dynamics, thermodynamics, and phase transitions in molecular systems. He leads efforts to develop advanced algorithms for simulating phase changes in complex systems, including work supported by a National Science Foundation (NSF) grant (CH-1114676) to improve computational methods for phase transition modeling. His group has pioneered generalized simulated tempering and replica exchange algorithms, enabling more accurate simulations of phenomena like vapor-liquid phase changes and peptide aggregation. Dr. Straub also engages in science outreach through collaborations with the Pinhead Institute, supporting K-12 education programs and student internships. His research spans diverse topics such as cholesterol interactions in lipid membranes, amyloid fibril formation mechanisms, and the structural basis of protein aggregation in neurodegenerative diseases. His computational methods have been applied to study membrane proteins, lipid rafts, and the role of environmental factors in protein behavior. Key contributions include modeling amyloid-β aggregation pathways and investigating the impact of membrane composition on protein stability.

• Theoretical Chemistry
• Computational Biophysics
• Protein Dynamics
• +3 more