Year |
Citation |
Score |
2024 |
Narkhede Y, Saxena R, Sharma T, Conarty JP, Ramirez VT, Motsa BB, Amiar S, Li S, Chapagain PP, Wiest O, Stahelin RV. Computational and experimental identification of keystone interactions in Ebola virus matrix protein VP40 dimer formation. Protein Science : a Publication of the Protein Society. 33: e4978. PMID 38591637 DOI: 10.1002/pro.4978 |
0.348 |
|
2024 |
Cioffi MD, Husby ML, Gerstman BS, Stahelin RV, Chapagain PP. Role of phosphatidic acid lipids on plasma membrane association of the Ebola virus matrix protein VP40. Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids. 1869: 159464. PMID 38360201 DOI: 10.1016/j.bbalip.2024.159464 |
0.61 |
|
2024 |
Johnson KA, Budicini MR, Bhattarai N, Sharma T, Urata S, Gerstman BS, Chapagain PP, Li S, Stahelin RV. PI(4,5)P binding sites in the Ebola virus matrix protein VP40 modulate assembly and budding. Journal of Lipid Research. 100512. PMID 38295986 DOI: 10.1016/j.jlr.2024.100512 |
0.62 |
|
2023 |
Sharma T, Gerstman B, Chapagain P. Distinctive Features of the XBB.1.5 and XBB.1.16 Spike Protein Receptor-Binding Domains and Their Roles in Conformational Changes and Angiotensin-Converting Enzyme 2 Binding. International Journal of Molecular Sciences. 24. PMID 37628766 DOI: 10.3390/ijms241612586 |
0.598 |
|
2023 |
Narkhede YB, Bhardwaj A, Motsa BB, Saxena R, Sharma T, Chapagain PP, Stahelin RV, Wiest O. Elucidating Residue-Level Determinants Affecting Dimerization of Ebola Virus Matrix Protein Using High-Throughput Site Saturation Mutagenesis and Biophysical Approaches. The Journal of Physical Chemistry. B. PMID 37458567 DOI: 10.1021/acs.jpcb.3c01759 |
0.337 |
|
2022 |
Baral P, Pavadai E, Zhou Z, Xu Y, Tison CK, Pokhrel R, Gerstman BS, Chapagain PP. Immunoinformatic screening of Marburgvirus epitopes and computational investigations of epitope-allele complexes. International Immunopharmacology. 111: 109109. PMID 35926269 DOI: 10.1016/j.intimp.2022.109109 |
0.529 |
|
2022 |
Hossen ML, Baral P, Sharma T, Gerstman B, Chapagain P. Significance of the RBD mutations in the SARS-CoV-2 omicron: from spike opening to antibody escape and cell attachment. Physical Chemistry Chemical Physics : Pccp. 24: 9123-9129. PMID 35395667 DOI: 10.1039/d2cp00169a |
0.546 |
|
2022 |
Pandey P, Bhattarai N, Su L, Wang X, Leng F, Gerstman B, Chapagain PP, He J. Detecting Individual Proteins and Their Surface Charge Variations in Solution by the Potentiometric Nanoimpact Method. Acs Sensors. 7: 555-563. PMID 35060380 DOI: 10.1021/acssensors.1c02385 |
0.586 |
|
2021 |
Pokhrel R, Bhattarai N, Baral P, Gerstman BS, Park JH, Handfield M, Chapagain PP. Lipid II Binding and Transmembrane Properties of Various Antimicrobial Lanthipeptides. Journal of Chemical Theory and Computation. PMID 34874159 DOI: 10.1021/acs.jctc.1c00666 |
0.566 |
|
2021 |
Bhattarai N, Pavadai E, Pokhrel R, Baral P, Hossen ML, Stahelin RV, Chapagain PP, Gerstman BS. Ebola Virus Protein VP40 Binding to Sec24c for Transport to the Plasma Membrane. Proteins. PMID 34431571 DOI: 10.1002/prot.26221 |
0.62 |
|
2021 |
Baral P, Bhattarai N, Hossen ML, Stebliankin V, Gerstman BS, Narasimhan G, Chapagain PP. Mutation-induced changes in the receptor-binding interface of the SARS-CoV-2 Delta variant B.1.617.2 and implications for immune evasion. Biochemical and Biophysical Research Communications. 574: 14-19. PMID 34425281 DOI: 10.1016/j.bbrc.2021.08.036 |
0.546 |
|
2021 |
Johnson KA, Bhattarai N, Budicini MR, LaBonia CM, Baker SCB, Gerstman BS, Chapagain PP, Stahelin RV. Cysteine Mutations in the Ebolavirus Matrix Protein VP40 Promote Phosphatidylserine Binding by Increasing the Flexibility of a Lipid-Binding Loop. Viruses. 13. PMID 34372582 DOI: 10.3390/v13071375 |
0.61 |
|
2021 |
Bhattarai N, Baral P, Gerstman BS, Chapagain PP. Structural and Dynamical Differences in the Spike Protein RBD in the SARS-CoV-2 Variants B.1.1.7 and B.1.351. The Journal of Physical Chemistry. B. PMID 34110159 DOI: 10.1021/acs.jpcb.1c01626 |
0.587 |
|
2021 |
Amiar S, Husby ML, Wijesinghe KJ, Angel S, Bhattarai N, Gerstman BS, Chapagain PP, Li S, Stahelin RV. Lipid-specific oligomerization of the Marburg virus matrix protein VP40 is regulated by two distinct interfaces for virion assembly. The Journal of Biological Chemistry. 100796. PMID 34019871 DOI: 10.1016/j.jbc.2021.100796 |
0.62 |
|
2020 |
Johnson KA, Pokhrel R, Budicini MR, Gerstman BS, Chapagain PP, Stahelin RV. A Conserved Tryptophan in the Ebola Virus Matrix Protein C-Terminal Domain Is Required for Efficient Virus-Like Particle Formation. Pathogens (Basel, Switzerland). 9. PMID 32455873 DOI: 10.3390/Pathogens9050402 |
0.67 |
|
2020 |
Baral P, Pavadai E, Gerstman BS, Chapagain PP. In-silico identification of the vaccine candidate epitopes against the Lassa virus hemorrhagic fever. Scientific Reports. 10: 7667. PMID 32376973 DOI: 10.1038/S41598-020-63640-1 |
0.591 |
|
2020 |
Wijesinghe KJ, McVeigh L, Husby ML, Bhattarai N, Ma J, Gerstman BS, Chapagain PP, Stahelin RV. Mutation of Hydrophobic Residues in the C-Terminal Domain of the Marburg Virus Matrix Protein VP40 Disrupts Trafficking to the Plasma Membrane. Viruses. 12. PMID 32344654 DOI: 10.3390/V12040482 |
0.669 |
|
2020 |
Pokhrel R, Pavadai E, Gerstman B, Chapagain PP. Ion Selective Pentameric Pore Formation by Ebola Virus Delta Peptide Biophysical Journal. 118: 586a-587a. DOI: 10.1016/J.Bpj.2019.11.3181 |
0.587 |
|
2020 |
Bhattarai N, Gerstman BS, Chapagain PP. Computational Study of the Molecular Details of Ebola Virus Matrix Protein VP40 and Human Sec24C Protein Interaction Biophysical Journal. 118: 506a. DOI: 10.1016/J.Bpj.2019.11.2787 |
0.645 |
|
2020 |
Baral P, Pavadai E, Gerstman B, Chapagain PP. Lassa Virus Epitope-Allele Complexes Identified through Computational Modeling Biophysical Journal. 118: 305a. DOI: 10.1016/J.Bpj.2019.11.1727 |
0.584 |
|
2020 |
Hossen ML, Chapagain PP, Gerstman B. Calculating the Binding Free Energy Difference between Conformational Changes of AT-Rich DNA Sequences Biophysical Journal. 118: 218a. DOI: 10.1016/J.Bpj.2019.11.1295 |
0.588 |
|
2019 |
Pavadai E, Bhattarai N, Baral P, Stahelin RV, Chapagain PP, Gerstman BS. Conformational Flexibility of the Protein-Protein Interfaces of the Ebola Virus VP40 Structural Matrix Filament. The Journal of Physical Chemistry. B. PMID 31576755 DOI: 10.1021/Acs.Jpcb.9B04674 |
0.679 |
|
2019 |
Pokhrel R, Bhattarai N, Baral P, Gerstman BS, Park JH, Handfield M, Chapagain PP. Molecular mechanisms of pore formation and membrane disruption by the antimicrobial lantibiotic peptide Mutacin 1140. Physical Chemistry Chemical Physics : Pccp. PMID 31147666 DOI: 10.1039/C9Cp01558B |
0.605 |
|
2019 |
Gerstman BS, Chapagain PP, Gc J, Steckmann T. Molecular Dynamics Simulations of Conformational Conversions in Transformer Proteins. Methods in Molecular Biology (Clifton, N.J.). 1958: 297-311. PMID 30945225 DOI: 10.1007/978-1-4939-9161-7_15 |
0.661 |
|
2019 |
Pokhrel R, Pavadai E, Gerstman BS, Chapagain PP. Membrane pore formation and ion selectivity of the Ebola virus delta peptide. Physical Chemistry Chemical Physics : Pccp. PMID 30785432 DOI: 10.1039/C8Cp07323F |
0.629 |
|
2019 |
Pokhrel R, Gerstman BS, Hutcheson JD, Chapagain PP. Computational Study of Calcium Phosphate Mineralization in Extracellular Vesicles Biophysical Journal. 116: 572a. DOI: 10.1016/J.Bpj.2018.11.3075 |
0.544 |
|
2019 |
Dhakal C, Chapagain P, Wang X. Temperature Dependence of the Protein-Chromophore Hydrogen Bond Dynamics in the Far-Red Fluorescent Proteins mNeptune1, mNeptune2.5 and mCardinal2 Biophysical Journal. 116: 475a. DOI: 10.1016/J.Bpj.2018.11.2564 |
0.337 |
|
2019 |
Pavadai E, Bhattarai N, Chapagain PP, Gerstman BS. Dynamics of the Protein Interfaces of the Ebola Virus VP40 Structural Matrix Filament Biophysical Journal. 116: 472a. DOI: 10.1016/J.Bpj.2018.11.2549 |
0.647 |
|
2019 |
Baral P, Bhattarai N, Pokhrel R, Gerstman B, Chapagain PP. Molecular Dynamics Investigations of Enzyme Conformational Changes Biophysical Journal. 116: 186a. DOI: 10.1016/J.Bpj.2018.11.1031 |
0.598 |
|
2019 |
Bhattarai N, Chapagain PP, Gerstman B. Molecular Basis of the Marburg Virus Protein VP24 Interactions with Human Keap1 Biophysical Journal. 116: 182a. DOI: 10.1016/J.Bpj.2018.11.1011 |
0.638 |
|
2018 |
Pavadai E, Gerstman BS, Chapagain PP. A cylindrical assembly model and dynamics of the Ebola virus VP40 structural matrix. Scientific Reports. 8: 9776. PMID 29950600 DOI: 10.1038/S41598-018-28077-7 |
0.678 |
|
2018 |
Pokhrel R, Gerstman BS, Hutcheson JD, Chapagain PP. In Silico Investigations of Calcium Phosphate Mineralization in Extracellular Vesicles. The Journal of Physical Chemistry. B. PMID 29519123 DOI: 10.1021/Acs.Jpcb.8B00169 |
0.587 |
|
2018 |
Del Vecchio K, Frick CT, Gc JB, Oda SI, Gerstman BS, Saphire EO, Chapagain PP, Stahelin RV. A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine. The Journal of Biological Chemistry. PMID 29348171 DOI: 10.1074/Jbc.M117.816280 |
0.671 |
|
2018 |
Pokhrel R, Sompornpisut P, Chapagain P, Olson B, Gerstman B, Pandey RB. Domain rearrangement and denaturation in Ebola virus protein VP40 Aip Advances. 8: 125129. DOI: 10.1063/1.5063474 |
0.689 |
|
2018 |
Pavadai E, Gerstman BS, Chapagain PP. A Cylindrical Assembly Model and Dynamics of the Ebola Virus VP40 Biophysical Journal. 114: 64a. DOI: 10.1016/J.Bpj.2017.11.399 |
0.611 |
|
2018 |
Bhattarai N, Chapagain PP, Gerstman BS. Conformational Changes in Marburg Virus VP40 upon Plasma Membrane Association Biophysical Journal. 114: 459a. DOI: 10.1016/J.Bpj.2017.11.2536 |
0.609 |
|
2018 |
Pokhrel R, GC J, Bhattarai N, Chapagain P, Gerstman B. Potential Disruption of Ebola Virus Matrix by Graphene Nano-Sheets Biophysical Journal. 114: 218a. DOI: 10.1016/J.Bpj.2017.11.1217 |
0.57 |
|
2017 |
Gc JB, Pokhrel R, Bhattarai N, Johnson KA, Gerstman BS, Stahelin RV, Chapagain PP. Graphene-VP40 interactions and potential disruption of the Ebola virus matrix filaments. Biochemical and Biophysical Research Communications. PMID 28917841 DOI: 10.1016/J.Bbrc.2017.09.052 |
0.606 |
|
2017 |
Gc JB, Gerstman BS, Chapagain PP. Membrane Association and Localization Dynamics of the Ebola Virus Matrix Protein VP40. Biochimica Et Biophysica Acta. PMID 28711356 DOI: 10.1016/J.Bbamem.2017.07.007 |
0.666 |
|
2017 |
Bhattarai N, Gc JB, Gerstman BS, Stahelin RV, Chapagain PP. Plasma membrane association facilitates conformational changes in the Marburg virus protein VP40 dimer. Rsc Advances. 7: 22741-22748. PMID 28580138 DOI: 10.1039/C7Ra02940C |
0.66 |
|
2017 |
Steckmann T, Bhandari YR, Chapagain PP, Gerstman BS. Cooperative structural transitions in amyloid-like aggregation. The Journal of Chemical Physics. 146: 135103. PMID 28390382 DOI: 10.1063/1.4979516 |
0.785 |
|
2017 |
Wijesinghe KJ, Urata S, Bhattarai N, Kooijman EE, Gerstman BS, Chapagain PP, Li S, Stahelin RV. Detection of Lipid Induced Structural Changes of the Marburg Virus Matrix Protein VP40 Using Hydrogen/Deuterium Exchange Mass Spectrometry. The Journal of Biological Chemistry. PMID 28167534 DOI: 10.1074/Jbc.M116.758300 |
0.657 |
|
2017 |
GC JB, Gerstman BS, Chapagain PP. Pi(4,5)P 2 Clustering by the Ebola Virus Matrix Protein VP40 Biophysical Journal. 112: 326a. DOI: 10.1016/J.Bpj.2016.11.1765 |
0.64 |
|
2017 |
Peña-Flores NL, Uzcategui C, Steckmann T, Chapagain P, Gerstman B. Temperature Dependent Pair-Wise Amino Acid Structural Propensity in ccβ and Implications for α to β Secondary Structural Conversion Biophysical Journal. 112: 191a. DOI: 10.1016/J.Bpj.2016.11.1059 |
0.648 |
|
2016 |
Gc JB, Gerstman BS, Stahelin RV, Chapagain PP. The Ebola virus protein VP40 hexamer enhances the clustering of PI(4,5)P2 lipids in the plasma membrane. Physical Chemistry Chemical Physics : Pccp. 18: 28409-28417. PMID 27757455 DOI: 10.1039/C6Cp03776C |
0.635 |
|
2016 |
Tiwari PB, Chapagain PP, Banda S, Darici Y, Üren A, Tse-Dinh YC. Characterization of molecular interactions between E. coli RNA polymerase and topoisomerase I by molecular simulations. Febs Letters. PMID 27448274 DOI: 10.1002/1873-3468.12321 |
0.322 |
|
2016 |
Konold PE, Yoon E, Lee J, Allen S, Chapagain PP, Gerstman BS, Regmi CK, Piatkevich KD, Verkhusha VV, Joo T, Jimenez R. Fluorescence from Multiple Chromophore Hydrogen-Bonding States in the Far-Red Protein TagRFP675. The Journal of Physical Chemistry Letters. PMID 27447848 DOI: 10.1021/Acs.Jpclett.6B01172 |
0.617 |
|
2016 |
Gc JB, Johnson KA, Husby ML, Frick CT, Gerstman BS, Stahelin RV, Chapagain PP. Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization. Protein Science : a Publication of the Protein Society. PMID 27328459 DOI: 10.1002/Pro.2969 |
0.666 |
|
2016 |
Fulcrand G, Dages S, Zhi X, Chapagain P, Gerstman BS, Dunlap D, Leng F. DNA supercoiling, a critical signal regulating the basal expression of the lac operon in Escherichia coli. Scientific Reports. 6: 19243. PMID 26763930 DOI: 10.1038/Srep19243 |
0.56 |
|
2016 |
gc jB, Gerstman BS, Chapagain PP. Interdomain Interactions and the Mechanism of Structural Transformation in RfaH Biophysical Journal. 110: 378a. DOI: 10.1016/J.Bpj.2015.11.2040 |
0.658 |
|
2016 |
Chapagain P, Regmi C, Gerstman B. On the Origin of the Extended Stoke's Shifts in Fluorescent Proteins Biophysical Journal. 110: 377a-378a. DOI: 10.1016/J.Bpj.2015.11.2039 |
0.597 |
|
2015 |
GC JB, Gerstman BS, Chapagain PP. The Role of the Interdomain Interactions on RfaH Dynamics and Conformational Transformation. The Journal of Physical Chemistry. B. 119: 12750-9. PMID 26374226 DOI: 10.1021/Acs.Jpcb.5B05681 |
0.654 |
|
2015 |
Chemmama IE, Chapagain PP, Gerstman BS. Pairwise amino acid secondary structural propensities. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 91: 042709. PMID 25974529 DOI: 10.1103/Physreve.91.042709 |
0.607 |
|
2015 |
Pham K, Dhulipala G, Gonzalez WG, Gerstman BS, Regmi C, Chapagain PP, Miksovska J. Ca2+ and Mg2+ modulate conformational dynamics and stability of downstream regulatory element antagonist modulator. Protein Science : a Publication of the Protein Society. 24: 741-51. PMID 25627705 DOI: 10.1002/Pro.2646 |
0.597 |
|
2015 |
Dean KM, Lubbeck JL, Davis LM, Regmi CK, Chapagain PP, Gerstman BS, Jimenez R, Palmer AE. Microfluidics-based selection of red-fluorescent proteins with decreased rates of photobleaching. Integrative Biology : Quantitative Biosciences From Nano to Macro. 7: 263-73. PMID 25477249 DOI: 10.1039/C4Ib00251B |
0.6 |
|
2015 |
Chemmama IE, Chapagain PP, Gerstman BS. Publisher's Note: Pairwise amino acid secondary structural propensities [Phys. Rev. E91, 042709 (2015)] Physical Review E. 91. DOI: 10.1103/Physreve.91.049902 |
0.579 |
|
2015 |
Chapagain P, Regmi CK, Gerstman BS. Hydrogen Bond Flexibility and Water Dynamics in the Far Red Fluorescent Protein TagRFP675 Biophysical Journal. 108: 469a. DOI: 10.1016/J.Bpj.2014.11.2562 |
0.597 |
|
2014 |
Gc JB, Bhandari YR, Gerstman BS, Chapagain PP. Molecular dynamics investigations of the α-helix to β-barrel conformational transformation in the RfaH transcription factor. The Journal of Physical Chemistry. B. 118: 5101-8. PMID 24758259 DOI: 10.1021/Jp502193V |
0.781 |
|
2014 |
Konold P, Regmi CK, Chapagain PP, Gerstman BS, Jimenez R. Hydrogen bond flexibility correlates with Stokes shift in mPlum variants. The Journal of Physical Chemistry. B. 118: 2940-8. PMID 24611679 DOI: 10.1021/Jp412371Y |
0.618 |
|
2014 |
Regmi CK, Chapagain PP, Gerstman BS. Temperature Dependence of the Protein-Chromophore Hydrogen Bond Dynamics in the Far-Red Fluorescent Protein Mplum Biophysical Journal. 106: 649a. DOI: 10.1016/J.Bpj.2013.11.3592 |
0.617 |
|
2013 |
Regmi CK, Bhandari YR, Gerstman BS, Chapagain PP. Exploring the diffusion of molecular oxygen in the red fluorescent protein mCherry using explicit oxygen molecular dynamics simulations. The Journal of Physical Chemistry. B. 117: 2247-53. PMID 23363049 DOI: 10.1021/Jp308366Y |
0.771 |
|
2013 |
Gerstman BS, Chapagain PP. Computational simulations of protein folding to engineer amino acid sequences to encourage desired supersecondary structure formation. Methods in Molecular Biology (Clifton, N.J.). 932: 191-204. PMID 22987354 DOI: 10.1007/978-1-62703-065-6_12 |
0.656 |
|
2012 |
Chemmama IE, Pelea AC, Bhandari YR, Chapagain PP, Gerstman BS. Structural propensities and entropy effects in peptide helix-coil transitions. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 86: 031915. PMID 23030952 DOI: 10.1103/Physreve.86.031915 |
0.779 |
|
2012 |
Laurent AD, Mironov VA, Chapagain PP, Nemukhin AV, Krylov AI. Exploring structural and optical properties of fluorescent proteins by squeezing: modeling high-pressure effects on the mStrawberry and mCherry red fluorescent proteins. The Journal of Physical Chemistry. B. 116: 12426-40. PMID 22988813 DOI: 10.1021/Jp3060944 |
0.351 |
|
2012 |
Bhandari YR, Chapagain PP, Gerstman BS. Lattice model simulations of the effects of the position of a peptide trigger segment on helix folding and dimerization. The Journal of Chemical Physics. 137: 105103. PMID 22979897 DOI: 10.1063/1.4752247 |
0.797 |
|
2012 |
Steckmann T, Awan Z, Gerstman BS, Chapagain PP. Kinetics of peptide secondary structure conversion during amyloid β-protein fibrillogenesis. Journal of Theoretical Biology. 301: 95-102. PMID 22586726 DOI: 10.1016/J.Jtbi.2012.02.012 |
0.621 |
|
2011 |
Chapagain PP, Regmi CK, Castillo W. Fluorescent protein barrel fluctuations and oxygen diffusion pathways in mCherry. The Journal of Chemical Physics. 135: 235101. PMID 22191901 DOI: 10.1063/1.3660197 |
0.336 |
|
2011 |
Chapagain PP, Gerstman BS, Bhandari YR, Rimal D. Free-energy landscapes and thermodynamic parameters of complex molecules from nonequilibrium simulation trajectories. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 83: 061905. PMID 21797401 DOI: 10.1103/Physreve.83.061905 |
0.767 |
|
2010 |
Liu Y, Chapagain PP, Gerstman BS. Stabilization of native and non-native structures by salt bridges in a lattice model of the GCN4 leucine dimer. The Journal of Physical Chemistry. B. 114: 796-803. PMID 20038147 DOI: 10.1021/Jp909872A |
0.635 |
|
2008 |
Gerstman BS, Chapagain PP. Self-organizing dynamics in protein folding. Progress in Molecular Biology and Translational Science. 84: 1-37. PMID 19121698 DOI: 10.1016/S0079-6603(08)00401-7 |
0.616 |
|
2008 |
Chapagain PP, Liu Y, Gerstman BS. The trigger sequence in the GCN4 leucine zipper: alpha-helical propensity and multistate dynamics of folding and dimerization. The Journal of Chemical Physics. 129: 175103. PMID 19045375 DOI: 10.1063/1.3006421 |
0.607 |
|
2008 |
Liu Y, Chapagain PP, Parra JL, Gerstman BS. Lattice model simulation of interchain protein interactions and the folding dynamics and dimerization of the GCN4 Leucine zipper. The Journal of Chemical Physics. 128: 045106. PMID 18248013 DOI: 10.1063/1.2831513 |
0.736 |
|
2008 |
Liu Y, Chapagain PP, Parra JL, Gerstman BS. Publisher’s Note: “Lattice model simulation of interchain protein interactions and the folding dynamics and dimerization of the GCN4 Leucine zipper” [J. Chem. Phys. 128, 045106 (2008)] The Journal of Chemical Physics. 128: 129901. DOI: 10.1063/1.2898870 |
0.722 |
|
2007 |
Chapagain PP, Parra JL, Gerstman BS, Liu Y. Sampling of states for estimating the folding funnel entropy and energy landscape of a model alpha-helical hairpin peptide. The Journal of Chemical Physics. 127: 075103. PMID 17718634 DOI: 10.1063/1.2757172 |
0.698 |
|
2006 |
Chapagain PP, Gerstman BS. Removal of kinetic traps and enhanced protein folding by strategic substitution of amino acids in a model alpha-helical hairpin peptide. Biopolymers. 81: 167-78. PMID 16215990 DOI: 10.1002/Bip.20388 |
0.646 |
|
2005 |
Gerstman BS, Chapagain PP. Self-organization in protein folding and the hydrophobic interaction. The Journal of Chemical Physics. 123: 054901. PMID 16108687 DOI: 10.1063/1.1990110 |
0.646 |
|
2004 |
Chapagain PP, Gerstman BS. Excluded volume entropic effects on protein unfolding times and intermediary stability. The Journal of Chemical Physics. 120: 2475-81. PMID 15268389 DOI: 10.1063/1.1637032 |
0.643 |
|
2003 |
Chapagain PP, Gerstman BS. Finite size scaling of structural transitions in a simulated protein with secondary and tertiary structure Journal of Chemical Physics. 119: 1174-1180. DOI: 10.1063/1.1579673 |
0.621 |
|
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