Research Topics
Species | Hyunbum JangSummaryAffiliation: National Cancer Institute Country: USA Publications
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Detail Information
Publications
Multiple pathways in conformational transitions of the alanine dipeptide: an application of dynamic importance samplingHyunbum Jang
Department of Physiology, Johns Hopkins University, Baltimore, Maryland 21205, USA
J Comput Chem 27:1136-41. 2006..The DIMS method represents an important step towards finding multiple transition pathways within complex biomolecular systems...
Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channelsHyunbum Jang
Center for Cancer Research Nanobiology Program, NCI Frederick, SAIC Frederick, Frederick, Maryland, USA
Biophys J 95:4631-42. 2008..Consistent with the toxic beta-amyloid channels that are ion-conducting, the PG-1 channels permeate anions...
Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effectHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick, Inc, NCI Frederick, Frederick, Maryland 21702, USA
BMC Struct Biol 7:21. 2007..The experimental structure of the PG-1 dimer is currently unavailable...
Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional linkHyunbum Jang
Center for Cancer Research Nanobiology Program, National Cancer Institute Frederick, SAIC Frederick, Frederick, Maryland, USA
Biophys J 100:1775-83. 2011..These combined properties support a functional relationship between amyloidogenic peptides and β-sheet-rich cytolytic AMPs, suggesting that amyloids channels may have an antimicrobial function...
Structural convergence among diverse, toxic beta-sheet ion channelsHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick, Inc, NCI Frederick, Frederick, Maryland 21702, USA
J Phys Chem B 114:9445-51. 2010....
Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavitiesJie Zheng
Basic Research Program, SAIC Frederick Center for Cancer Research, Nanobiology Program, NCI Frederick, Frederick, Maryland 21702, USA
Biophys J 93:3046-57. 2007..Thus, we propose that Abeta fiber architecture consists of alternating layers of tight packing and hydrated cavities running along the fibrillar axis, which might be possibly detected by high-resolution imaging...
Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndromeHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick, Inc, National Cancer Institute, Frederick, MD 21702, USA
Proc Natl Acad Sci U S A 107:6538-43. 2010..The toxicity of nonamyloidogenic peptides via an ion channel mechanism necessitates a reevaluation of the current therapeutic approaches targeting the nonamyloidogenic pathway as avenue for AD treatment...
Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channelsHyunbum Jang
Center for Cancer Research Nanobiology Program, NCI Frederick, SAIC Frederick, Frederick, Maryland, USA
Biophys J 97:3029-37. 2009..Nature designs folded channels but not misfolded toxic channels...
β-Barrel topology of Alzheimer's β-amyloid ion channelsHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick, Inc, National Cancer Institute Frederick, Frederick, MD 21702, USA
J Mol Biol 404:917-34. 2010..The subunits appear mobile, allowing unregulated, hence toxic, ion flux...
How to lose a kink and gain a helix: pH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayersHyunbum Jang
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Proteins 72:299-312. 2008..This conformational change is pH-independent, and is closely related to the peptide insertion into the lipid bilayer...
Interaction of protegrin-1 with lipid bilayers: membrane thinning effectHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC-Frederick, Inc, NCI-Frederick, Frederick, Maryland 21702, USA
Biophys J 91:2848-59. 2006..The thinning effects in the bilayer should relate to pore/channel formation in the lipid bilayer and thus be responsible for further defects in the membrane caused by oligomer...
Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic processHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick, National Cancer Institute Frederick, Frederick, MD 21702, USA
Biophys J 93:1938-49. 2007..The observed loosely connected subunit organization suggests that amyloid channel formation in the bilayer is a dynamic, fluid process involving subunit association, dissociation, and channel rearrangements...
New structures help the modeling of toxic amyloidbeta ion channelsHyunbum Jang
Center for Cancer Research Nanobiology Program, SAIC Frederick Inc NCI Frederick, Frederick, MD 21702, USA
Trends Biochem Sci 33:91-100. 2008..Molecular dynamics modeling can provide blueprints of 3D structural conformations for many other amyloids whose membrane association is key to their toxicity...
How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensationHyunbum Jang
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Biophys J 87:129-45. 2004....
Material properties of matrix lipids determine the conformation and intermolecular reactivity of diacetylenic phosphatidylcholine in the lipid bilayerAnu Puri
Membrane Structure and Function Section, SAIC Frederick, Inc, Nanobiology Program, Center for Cancer Research, Frederick, Maryland 21702, USA
Langmuir 27:15120-8. 2011..These results show that the DC(8,9)PC molecules cluster and assume the preferred conformation in the gel-phase matrix for the UV-triggered polymerization reaction...
Tools for channels: moving towards molecular calculations of gating and permeation in ion channel biophysicsThomas B Woolf
Department of Physiology, Johns Hopkins University, School of Medicine, Biophysics 206, 725 N Wolfe Street, Baltimore, MD 21205, USA
J Mol Graph Model 22:359-68. 2004....
Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsHyunbum Jang
Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, USA
Biophys J 86:31-49. 2004....
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42Jie Zheng
Department of Chemical and Biomolecular Engineering, The University of Akron, Akron, Ohio 44325, USA
J Phys Chem B 112:6856-65. 2008....
Thermodynamics and stability of a beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsHyunbum Jang
Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, USA
Protein Sci 13:40-53. 2004..The highly ordered beta-sheet complex has fully-stiff beta-sheet strands, the same as the global energy minimum structure, and is observed for all eta at low temperatures...
Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specificJie Zheng
Department of Chemical and Biomolecular Engineering, The University of Akron, Akron, Ohio 44325, USA
Biochemistry 47:2497-509. 2008....
Folding thermodynamics of model four-strand antiparallel beta-sheet proteinsHyunbum Jang
Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695 7905, USA
Biophys J 82:646-59. 2002..However the low temperature transitions, i.e., the folding transition and the liquid-to-solid transition, strongly depend on the native-state geometry of the model proteins and the size of the bias gap...
Protein folding pathways and kinetics: molecular dynamics simulations of beta-strand motifsHyunbum Jang
Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695, USA
Biophys J 83:819-35. 2002..The kinetic folding behavior of the beta-strand proteins strongly depends on the native-state geometry of the model proteins and the size of the bias gap g, an artificial measure of a model protein's preference for its native state...
