جست‌وجوی استاد و پژوهشگر

John Straubمشاهده پروفایل

استاد

• Theoretical Chemistry
• Computational Biophysics
• Protein Dynamics
• +۳ مورد دیگر

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.

John E. Straubمشاهده پروفایل

استاد

• Molecular Dynamics
• Thermodynamics
• Protein Aggregation
• +۷ مورد دیگر

John E. Straub is a Professor in the Department of Chemistry at Boston University (BU), where he leads the Straub Lab. His work focuses on molecular dynamics and thermodynamics of complex biomolecular systems, particularly protein aggregation and amyloid formation. He has authored influential books, including Proteins: Energy, Heat and Signal Flow and Mathematical Methods for Molecular Science , and has held leadership roles such as Chair of the Department of Chemistry at BU (2007-2012) and President of the Telluride Science Research Center (2006-2008). Education: BS in Chemistry (University of Maryland, 1982, advisor: Millard Alexander) MA (Columbia University, 1984) MPhil (Columbia University, 1986) PhD in Chemical Physics (Columbia University, 1987, advisor: Bruce Berne) NIH Postdoctoral Fellow in Chemistry (Harvard University, 1987-1990, advisor: Martin Karplus) His research interests span computational methods for enhanced sampling, reaction dynamics, and the interplay between protein structure and aggregation. He has pioneered studies on amyloid precursor proteins and cholesterol interactions in lipid bilayers, emphasizing the role of monomer structural ensembles in aggregation mechanisms. Articles from his lab highlight advancements in understanding lipid phase separation, amyloid fibril formation, and computational techniques like machine learning-derived variables and replica exchange methods. His work bridges theory and experiment, with collaborations across institutions globally. Scientific Awards: NIH Postdoctoral Fellowship (Harvard University, 1987-1990). Professor Straub has advised numerous students, many of whom hold academic positions at leading institutions, including Jianpeng Ma (Rice University) and Nicolae-Viorel Buchete (University College Dublin). His lab actively explores projects in computational biophysics, with ongoing work on lipid mixtures, sterol-derived Raman tags, and membrane protein interactions.

Ross Dalbeyمشاهده پروفایل

استاد

• Biochemistry
• Membrane Biology
• Proteins
• +۳ مورد دیگر

Dr. Ross Dalbey is a Full Professor in the Department of Chemistry and Biochemistry at The Ohio State University, affiliated with the College of Arts and Sciences. He holds a B.S. in Chemistry from the University of Washington (1978) and a Ph.D. in Biochemistry from Washington State University (1983). Postdoctoral training included work with Prof. William Wickner at UCLA. His research focuses on membrane protein assembly and proteases, particularly the YidC protein's role in membrane insertion and folding. Key areas include biophysical mechanisms of protein insertion, signal peptidase function, and mitochondrial membrane systems. He has held NIH and AAAS fellowships, and his lab has been funded by NIH and NSF for over three decades. His students hold academic and industry positions at institutions like NIH, MIT, and pharmaceutical companies such as Eli Lilly. Education: B.S., Chemistry, University of Washington, 1978 Ph.D., Biochemistry, Washington State University, 1983 Awards: American Cancer Society Junior Faculty Award (1989–1992) Elected Fellow of the American Association for the Advancement of Science (AAAS) Professional Memberships: American Chemical Society Federation of American Societies for Experimental Biology American Society of Microbiology Sigma Xi Phi Kappa Phi His lab investigates how proteins are inserted into membranes and folded, with emphasis on the YidC/Oxa1 family of insertases. Recent work explores YidC's substrate specificity, dimeric structure, and interactions with the Sec translocon. Studies on proteases like signal peptidase reveal their roles in membrane-associated peptide cleavage. Collaborations include structural biology with Prof. Horst Vogel in Switzerland and functional analyses with Prof. White at Ohio State. Research highlights include defining YidC's role in multispan membrane protein integration and uncovering evolutionary conservation across bacterial, archaeal, and eukaryotic systems. The lab's findings contribute to understanding mitochondrial protein insertion pathways and drug design targeting membrane-associated enzymes.

Dirk Schneiderمشاهده پروفایل

استاد

• Membrane Biochemistry
• Biophysics
• Protein-Lipid Interactions
• +۴ مورد دیگر

Prof. Dirk Schneider is a Full Professor (W3) of Biochemistry at Johannes Gutenberg University Mainz since 2010, with previous appointments at the University of Freiburg (2003-2009) and postdoctoral training at Yale University. His research spans membrane biochemistry, biophysics, and transmembrane protein folding/assembly, focusing on thylakoid membrane biogenesis and protein-lipid interactions in cyanobacteria and chloroplasts. Current roles: Full Professor, University Mainz Previous roles: Assistant Professor (W1), University of Freiburg Education: PhD (summa cum laude) from Ruhr-University Bochum His research interests include: Membrane protein folding and stability ESCRT-III/Vipp1/PspA family structural dynamics ABC transporter activity regulation (e.g., BmrA) Protein-lipid interaction mechanisms Thylakoid membrane remodeling Comparative membrane biology between prokaryotes and eukaryotes Development of spectroscopic and computational methods Recent publications reveal trends in bacterial membrane remodeling (SynDLP, PspA), lipid effects on transporter activity (BmrA), and IM30/Vipp1-mediated membrane fusion. His work combines structural biology, biophysics, and functional assays to elucidate membrane dynamics. Awarded the Dr. Heinrich Kost Award (2001) and Leopoldina Fellowship (2001) , he has held leadership roles including Study Section Speaker (2010-2014) , Director of Institute of Pharmacy and Biochemistry (2013-2015) , and Dean of Faculty of Chemistry (2015-2020) . His scientific advisory roles include editorial board memberships and study section leadership.

Elizabeth Sargentمشاهده پروفایل

استادیار

• Scholarship of Teaching and Learning
• Biogeochemistry
• Phytoplankton Ecophysiology
• +۱ مورد دیگر

Elizabeth Sargent serves as an Assistant Professor in the School of Marine Science and Policy within the College of Earth, Ocean and Environment at the University of Delaware. Her office is located in 112B Robinson Hall on the Newark campus, with primary contact through esargent@udel.edu. Her academic credentials include: Ph.D. in Biological Oceanography from the University of Southampton, National Oceanography Centre (2014) B.A. in Marine Biology from Roger Williams University (2009) Dr. Sargent's research spans Scholarship of Teaching and Learning (SoTL), biogeochemistry, phytoplankton ecophysiology, and algal ecology. Her recent scholarship demonstrates a strategic pivot from marine biogeochemistry toward educational innovation, with concentrated focus on developing and evaluating Course-based Undergraduate Research Experiences (CUREs) and the Remote Mentoring of Undergraduate Research Students (ReMentURS) framework. She investigates pedagogical effectiveness across instructional modalities while maintaining connections to marine science through earlier foundational work. Publication trends reveal a distinct transition from marine biogeochemistry (2011-2016) to educational research dominance (2018-2023), particularly in forensic chemistry CURE development, remote mentoring infrastructure, and assessment of flipped instruction techniques. Current work emphasizes evidence-based STEM education practices with strong focus on accessibility and mentorship scalability. Scientific Recognition: No formal awards documented in provided materials Dr. Sargent actively cultivates undergraduate research capacity through structured mentoring initiatives and curriculum innovation. Her ReMentURS program addresses critical gaps in remote research guidance, while forensic chemistry CURE development expands authentic research opportunities at primarily undergraduate institutions. She contributes significantly to faculty development through workshop series on mentoring best practices and evidence-based teaching strategies.

Kathy Iovineمشاهده پروفایل

استاد

• Developmental Biology
• Regeneration
• Skeletal Morphogenesis
• +۴ مورد دیگر

Kathy Iovine serves as Professor and Department Chair at Lehigh University, leading research in skeletal development and regeneration using zebrafish models. Her work focuses on elucidating molecular mechanisms controlling bone growth through fin regeneration studies. Her primary research interests span developmental biology, regeneration, skeletal morphogenesis, cell-cell communication, and extracellular matrix dynamics. She investigates how connexin43 (Cx43)-mediated gap junctional communication coordinates skeletal growth and patterning, with emphasis on segment addition in zebrafish fins as the fundamental unit of bone growth. Key areas include semaphorin signaling, hyaluronic acid metabolism, and collagen-based actinotrichia structures. Analysis of her publication record reveals consistent exploration of Cx43-dependent networks across 15+ recent studies. Her work demonstrates how mutations in connexin43 disrupt fin length regulation through effects on cell proliferation and joint formation, identifying critical mediators like Sema3d and Hapln1a. The research integrates genetic, molecular, and cellular approaches to dissect pathways governing skeletal morphogenesis. Dr. Iovine directs an active research laboratory investigating the genetic basis of skeletal development. Her team has characterized how actinotrichia integrity signals between proliferating and differentiating cell compartments to coordinate growth, and how Cx43 regulates extracellular environment modifiers. Current efforts focus on validating additional genes within the Cx43-dependent network to uncover novel therapeutic targets for skeletal disorders.

Natalie K. Gotoمشاهده پروفایل

دانشیار

• Protein Structure
• Protein Dynamics
• Solution NMR Spectroscopy
• +۵ مورد دیگر

Natalie K. Goto is an Associate Professor in the Department of Chemistry and Biomolecular Sciences at the University of Ottawa. She leads a research laboratory focused on protein science using solution NMR spectroscopy. Her educational background includes a B.Sc. in Biochemistry from the University of Toronto (1993), a Ph.D. from the University of Toronto (2001), and postdoctoral training at The Scripps Research Institute (2002). Her research investigates protein structure-function relationships in two primary areas: (1) Bacterial cell division mechanisms, particularly the MinCDE system in Neisseria gonorrhoeae that regulates symmetric cell division through membrane-associated oscillation; and (2) Membrane protein structural biology, with emphasis on rhomboid proteases like GlpG and their function in lipid bilayers. Her lab employs NMR spectroscopy to analyze protein dynamics and conformational changes. Professor Goto has received notable scientific recognition including the Ontario Early Researcher Award (2008), John Charles Polanyi Prize in Chemistry (2004), and Research Corporation Innovation Award (2003). She currently advises graduate students including Adam Cloutier (MSc) and Anwar Hassan (MSc), and is actively recruiting additional graduate students and postdoctoral researchers to her laboratory.

Nils Gunnar Hansson von Heijneمشاهده پروفایل

استاد

• Membrane Proteins
• Protein Folding
• Signal Peptides
• +۵ مورد دیگر

Nils Gunnar Hansson von Heijne is a Professor of Biochemistry at the Department of Biochemistry and Biophysics, Stockholm University. He leads a research group focused on membrane protein biogenesis and cotranslational protein folding mechanisms. His academic journey began with a PhD in Theoretical Physics from the Royal Institute of Technology, Stockholm (1980), followed by postdoctoral work at the University of Michigan. His career path includes Assistant Professor at KTH (1981-1988), Associate Professor at Karolinska Institutet (1989-1994), and Professor at Stockholm University since 1994. He has held significant leadership roles including Director of the Stockholm Bioinformatics Center (2000-2006), Director of the Center for Biomembrane Research (2006-2015), and Director of the SciLifeLab National Cryo-EM Facility (2016-2021). Professor von Heijne's research focuses on the fundamental mechanisms of protein folding and membrane insertion. His group pioneered the use of arrest peptides as molecular force sensors to measure the forces acting on nascent polypeptide chains during synthesis. His work spans membrane protein topology, cotranslational folding, signal peptide function, and the energetics of protein-membrane interactions. He has made significant contributions to understanding how the ribosome exit tunnel geometry affects protein folding and how transmembrane segments integrate into lipid bilayers. His publication record shows consistent high-impact contributions, with recent work emphasizing residue-by-residue analysis of membrane protein integration, cotranslational folding cooperativity in multidomain proteins, and the development of advanced prediction tools like SignalP 5.0 that utilize deep neural networks for signal peptide identification. As evidenced by his autobiographical article 'Membrane protein serendipity' (2018), von Heijne has served on the Nobel Committee for Chemistry and has embraced interdisciplinary approaches throughout his career, moving from theoretical physics to molecular biology through what he describes as 'serendipity' rather than careful planning.

Fabio Lolicatoمشاهده پروفایل

پژوهشگر

• Computational Biophysics
• Biomembrane Research
• Molecular Biology
• +۳ مورد دیگر

Dr. Fabio Lolicato is a Group Leader at the Biochemistry Center (BZH) , Heidelberg University, Germany. His research spans computational biophysics and biomembrane science, focusing on protein-lipid interactions, unconventional secretion, and membrane disruption mechanisms. He has held leadership roles since 2024 and previously served as a Principal Investigator (2023-2024). PhD in Computational Biophysics (University of Helsinki, 2016-2020) Post-doctoral research in Walter Nickel's lab (BZH, Heidelberg, 2019-2023) Active in scientific community as journal reviewer (2013-present) and conference organizer (2022) Dr. Lolicato's work integrates computational modeling with experimental approaches to study membrane dynamics, including protein translocation, lipid clustering, and viral fusion mechanisms. His publications highlight collaborations with interdisciplinary teams across Europe. Recent research trends include: Investigating FGF2 membrane translocation and unconventional secretion pathways Elucidating molecular mechanisms of influenza and Ebola virus entry Exploring apoptosis regulation through transmembrane domains Advancing structure-based drug design for amyloidogenic proteins Scientific Contributions: Key findings on cholesterol's role in PI(4,5)P2 clustering (2022) Identification of disulfide bridges in extracellular FGF2 release (2023) Discovery of IFITM3's lipid-sorting function against influenza (2023) Contact: Email: fabio.lolicato@bzh.uni-heidelberg.de Phone: +49 6221 54-4181 (Office), +49 6221 54-4746 (Lab) Address: Im Neuenheimer Feld 328, 69120 Heidelberg, Germany

Brian Craneمشاهده پروفایل

استاد

• Biophysical Chemistry
• Chemical Biology
• Bioinorganic Chemistry
• +۶ مورد دیگر

Brian Crane serves as the George W. and Grace L. Todd Professor in the Department of Chemistry and Chemical Biology at Cornell University's College of Arts and Sciences. His research focuses on the structural and mechanistic aspects of protein systems involved in biological signal transduction. PhD, The Scripps Research Institute BSc, University of Manitoba Crane's academic interests center on biophysical and chemical biology approaches to understanding: Protein electron transfer reactions Photochemical processes in biological systems Nitric oxide signaling and enzymology Redox-dependent signal transduction Macromolecular assembly dynamics His work spans circadian clock light sensors, bacterial transmembrane signaling, and nitric oxide-mediated stress responses, utilizing advanced methodologies like cryo-electron microscopy, electron spin resonance spectroscopy, and macromolecular crystallography. Crane has contributed to high-impact publications in journals including Science, Nature, and Cell.

Edwin Liمشاهده پروفایل

دانشیار

• Membrane Protein Biophysics
• Transmembrane Domain Dimerization
• Cell Signaling Mechanisms
• +۳ مورد دیگر

Edwin Li is an Associate Professor at Saint Joseph's University in the Department of Biology, Philadelphia, PA. His research focuses on membrane protein biophysics, particularly the structural and energetic principles governing transmembrane domain dimerization in receptor tyrosine kinases and mucin-type proteins. B.S. in Chemical Engineering, Rutgers University (1994) M.S. in Chemical Engineering, University of Rhode Island (1997) Ph.D. in Chemical Engineering, University of Rhode Island (2001) His laboratory investigates how mutations in transmembrane domains contribute to pathologies like dwarfism and cancer. Key methodologies include Förster Resonance Energy Transfer (FRET), surface-supported bilayers, and lipid bilayer systems to study protein interactions in physiologically relevant environments. Research trends across his publications highlight: structural analysis of FGFR3 and MUC1 dimerization, CQC motif roles in membrane protein self-assembly, lipid chain length effects on tetramer assembly, and quantitative measurements of protein interactions in crowded cellular environments.

Charles M. Deberمشاهده پروفایل

استاد

• Biochemistry
• Membrane Protein Structure
• Peptide Therapeutics
• +۴ مورد دیگر

Dr. Charles M. Deber is a Professor in the Department of Biochemistry at the University of Toronto, with a cross-appointment at the Research Institute of the Hospital for Sick Children since 1976. His work bridges biochemistry, molecular medicine, and biophysics. Research Focus: Dr. Deber investigates membrane protein structure and function, particularly how mutations in transmembrane segments lead to diseases like cystic fibrosis. His lab designs therapeutic peptides targeting bacterial resistance and membrane interactions. Awards & Honors: 2000 Vincent du Vigneaud Award (American Peptide Society) 2001 Fellow of the Royal Society of Canada (FRSC) 2009 Murray Goodman Award for Scientific Excellence 1996 W.T. Aikins Award for Teaching (University of Toronto) Academic Contributions: He has pioneered spectroscopic and computational methods to study membrane protein folding, developed novel antimicrobial peptides with patented charge-segregation designs, and mentored students through courses like BCH2024H and BCH473Y.

Harish Vashisthمشاهده پروفایل

استاد

• Computational Biophysics
• Chemical Physics
• Soft Matter and Self-assembly
• +۱۴ مورد دیگر

Harish Vashisth serves as Professor of Chemical Engineering & Bioengineering at the University of New Hampshire, where he teaches graduate courses including Advanced Chemical Engineering Thermodynamics and Computational Molecular Bioengineering. His research focuses on computational approaches to biomolecular problems with applications in therapeutic design and materials discovery. His educational background includes: Ph.D. in Chemical Engineering from Drexel University Bachelor of Technology in Chemical Engineering from National Institute of Technology Research Expertise: Dr. Vashisth specializes in Computational Biophysics, Chemical Physics, and Soft Matter Self-assembly. His laboratory employs molecular thermodynamics and statistical mechanics to investigate complex macromolecules including proteins, nucleic acids, and colloids. This work bridges fundamental biophysical principles with applications in drug design, biomaterials engineering, and artificial water channel development. Publication Trends: Analysis of 15 most recent publications (2023-2025) reveals dominant themes in viral peptide-receptor interactions, transmembrane domain dynamics, and light-responsive colloidal systems. His group consistently integrates molecular dynamics simulations with quantum chemistry methods, demonstrating strong interdisciplinary collaboration between computational and experimental approaches in biophysical chemistry. Scientific Recognition: No major awards or fellowships are documented in current profile Academic Leadership: Dr. Vashisth supervises doctoral research in chemical engineering and bioengineering, teaching core graduate courses while directing the Vashisth Research Group. His work has secured federal research funding for projects on biomolecular modeling and soft matter systems, particularly in biomimetic membrane development. Research Infrastructure: The Vashisth Research Group operates within UNH's Chemical Engineering & Bioengineering department, utilizing high-performance computing for molecular simulations. The lab collaborates extensively with experimental groups on projects involving artificial water channels, viral replication mechanisms, and novel biomaterials for Angstrom-scale separations.

• Supramolecular Chemistry
• Nanobiomimetics
• Molecular Biophysics
• +۴ مورد دیگر

Rebeca Garcia Fandiño is a Full Professor in the Department of Organic Chemistry at the Faculty of Biology, University of Santiago de Compostela. She leads the SupraNanoBioMol research group focused on supramolecular systems, nanobiomimetics and molecular biophysics. Develops cyclodextrin-based therapeutics for age-related diseases Studies cyclic peptide nanotubes for antimicrobial applications Specializes in molecular dynamics simulations of biomolecular systems Her research explores hierarchical membrane structures, water model effects in nanoconfined environments, and membrane-targeted therapies. She has published extensively on: Toxic oxysterol removal using cyclodextrin dimers Antimicrobial D,L-α-cyclic peptide interactions Quantum-classical simulation hybrid approaches Post-COVID condition molecular characterization Augmented reality applications in education The SupraNanoBioMol group at CIQUS center utilizes experimental and computational techniques including DSC, ATR-FTIR and MD simulations. Recent work addresses antimicrobial resistance through membrane disruption mechanisms and AI-driven drug discovery.

Brian Kobilkaمشاهده پروفایل

استاد

• G protein-coupled receptors (GPCRs)
• Adrenergic receptor biology
• Receptor structure
• +۵ مورد دیگر

Brian Kobilka is a Professor of Molecular and Cellular Physiology at Stanford University School of Medicine, holding the Hélène Irwin Fagan Chair of Cardiology. He is a member of multiple prestigious institutes including Bio-X, the Cardiovascular Institute, the Maternal & Child Health Research Institute (MCHRI), and the Wu Tsai Neurosciences Institute. Dr. Kobilka's research focuses on G protein-coupled receptors (GPCRs), particularly adrenergic receptors. His laboratory studies receptor structure, intracellular trafficking, and the physiological relevance of receptor subtype diversity. Using techniques like cryo-EM, molecular dynamics, and single-molecule imaging, his team investigates conformational changes during receptor activation and G protein coupling. His recent publications reveal groundbreaking insights into GPCR mechanisms, including G protein coupling specificity, receptor activation pathways, and novel drug design approaches for pain management and metabolic disorders. His work bridges structural biology with therapeutic applications, with particular emphasis on understanding how receptor conformational changes translate to specific signaling outcomes. Nobel Prize in Chemistry (2012) for studies of G protein-coupled receptors American Academy of Arts and Sciences (2010) National Academy of Sciences (2009) Dr. Kobilka mentors numerous postdoctoral scholars, doctoral students, and medical scholars. His laboratory has trained many successful scientists who continue to advance the field of receptor pharmacology. His research is supported by multiple NIH grants and other funding sources that enable cutting-edge structural and biophysical investigations of receptor function. The Kobilka Lab at Stanford employs cutting-edge techniques including time-resolved cryo-EM, single-molecule fluorescence imaging, and molecular dynamics simulations to study GPCR structure and function. The lab maintains strong collaborations with pharmaceutical companies and academic researchers worldwide, focusing on translating basic science discoveries into therapeutic applications for cardiovascular disease, pain management, and neurological disorders.