المؤلفون: Hongchul Shin, Taeyoung Yoon, Wooboum Park, Juneseok You, Sungsoo Na

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Biotechnology, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, Information Systems not elsewhere classified, β sheet structure, ultimate tensile strength, typical electrospinning machines, optimizing electrospinning processes, nephila clavipes <, mechanical property decrease, spider silk maintains, electrospun spider silk, nm electric field, spider silk, silk proteins, mechanical properties, electric fields, young ’, varying amplitudes, study opens, study investigated, study demonstrates, structural integrity, significantly influence, shedding light, power levels, particularly sensitive

Relation: https://figshare.com/articles/journal_contribution/Unraveling_the_Mechanical_Property_Decrease_of_Electrospun_Spider_Silk_A_Molecular_Dynamics_Simulation_Study/25303389

الاتاحة: https://doi.org/10.1021/acsabm.4c00046.s001
https://figshare.com/articles/journal_contribution/Unraveling_the_Mechanical_Property_Decrease_of_Electrospun_Spider_Silk_A_Molecular_Dynamics_Simulation_Study/25303389

المؤلفون: Souvik Misra (7489997), Pijush Singh (7489994), Rabindra Nath Mahata (10686779), Paula Brandão (1332606), Subhasish Roy (1407331), Ajit K. Mahapatra (10686782), Jayanta Nanda (2035552)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Neuroscience, Biotechnology, Computational Biology, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, acid-rich peptide fragments, FT-IR, electron-deficient carbonyl carbon, β- sheet conformation, electron-rich sp 3, Amyloid Sequence Self-assembly, β- sheet structure, antiparallel β- sheet fashion, β- sheet region, antiparallel β- sheet structure, crystal structure, β- sheet-like conformation

Relation: https://figshare.com/articles/journal_contribution/Supramolecular_Antiparallel_Sheet_Formation_by_Tetrapeptides_Based_on_Amyloid_Sequence/14466392

الاتاحة: https://doi.org/10.1021/acs.jpcb.0c10920.s001

المؤلفون: Jennifer A. Macdonald, Iraad F. Bronner, Lesley Drynan, Juan Fan, Annabelle Curry, Graham Fraser, Isabelle Lavenir, Michel Goedert

المصدر: Acta Neuropathologica Communications, Vol 7, Iss 1, Pp 1-11 (2019)

مصطلحات موضوعية: Tau assembly, Neurodegeneration, Tauopathy, β-Sheet structure, Tau filaments, Sarkosyl-insoluble tau, Neurology. Diseases of the nervous system, RC346-429

وصف الملف: electronic resource

Relation: http://link.springer.com/article/10.1186/s40478-019-0695-5; https://doaj.org/toc/2051-5960

URL الوصول: https://doaj.org/article/b5e78336638247b6b7a93dfe965c6c2a

المؤلفون: Ujjayini Ghosh (1578778), David P. Weliky (1344474)

مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Cell Biology, Science Policy, Infectious Diseases, Virology, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, pH 5, influenza, lipid acyl chains, large-amplitude motions, pH 7, antiparallel β sheet structure, membrane fusion intermediates, temperature dependence, 7. GPfp, membrane-enveloped virus, perdeuterated DMPC membrane, R 2 CD 2, 2 H NMR, HAfp, chain location, membrane liquid-crystalline-to-gel ., fusion catalysis, Catalyze Membrane Fusion, Bound Viral Fusion Peptide, vesicle fusion, nonhomologous HIV

Relation: https://figshare.com/articles/journal_contribution/Rapid_sup_2_sup_H_NMR_Transverse_Relaxation_of_Perdeuterated_Lipid_Acyl_Chains_of_Membrane_with_Bound_Viral_Fusion_Peptide_Supports_Large-Amplitude_Motions_of_These_Chains_That_Can_Catalyze_Membrane_Fusion/16455494

الاتاحة: https://doi.org/10.1021/acs.biochem.1c00316.s001

المؤلفون: Kengo Manabe (1437730), Emiko Koyama (1743151), Yasuo Norikane (1743139)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Molecular Biology, Physiology, Ecology, Hematology, Space Science, Environmental Sciences not elsewhere classified, Biological Sciences not elsewhere classified, food products, material, noncovalent polymer network, gas separation applications, ultrafast self-healing gas barrier ., oxygen transmission rate, nanobrick wall structures, packaging, Cephalopods-Inspired Rapid Self-Hea., lack repair performance, oxygen barrier properties, Super-Bubble-Phobic Properties Poly., montmorillonite, surface, technology, film, cephalopod-derived β- sheet structure

Relation: https://figshare.com/articles/journal_contribution/Cephalopods-Inspired_Rapid_Self-Healing_Nanoclay_Composite_Coatings_with_Oxygen_Barrier_and_Super-Bubble-Phobic_Properties/15025599

الاتاحة: https://doi.org/10.1021/acsami.1c09588.s001

المؤلفون: Bingyu Liu (3353852), Aiyou Hao (539139), Pengyao Xing (539138)

مصطلحات موضوعية: Biophysics, Biochemistry, Pharmacology, Biotechnology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, novel chiroptical switches, ferrocene, biomolecule, adaptive peptide-based biomaterials, dipeptide arm angles, Solid X-ray structures, transformation, β- sheet structure, hydration effect

Relation: https://figshare.com/articles/journal_contribution/Water-Mediated_Folding_Behaviors_and_Chiroptical_Inversion_of_Ferrocene-Conjugated_Dipeptides/14884691

الاتاحة: https://doi.org/10.1021/acs.jpclett.1c01231.s001

المؤلفون: Yujuan Cao (2416072), Zhenyan He (1922212), Yuting Gao (8108615), Yanru Xin (5729279), Liang Luo (425058), Fanling Meng (2257996)

مصطلحات موضوعية: Biophysics, Biochemistry, Neuroscience, Cancer, Environmental Sciences not elsewhere classified, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, Information Systems not elsewhere classified, amyloid aggregates, ultrastable β- sheet structure, IAPP aggregates, photodynamic degradation, strategy, ROS, TPCI, Multiple characterization studies, reactive oxygen species, Islet Amyloid Polypeptide Aggregate., islet amyloid polypeptide

Relation: https://figshare.com/articles/journal_contribution/Boosting_the_Photodynamic_Degradation_of_Islet_Amyloid_Polypeptide_Aggregates_Via_a_Bait-Hook-Devastate_Strategy/14312188

الاتاحة: https://doi.org/10.1021/acsami.1c00082.s001

المؤلفون: Subhashis Pal (1738093), Mohd Sayeed (8714721), Amit Kumar (81180), Devesh P. Verma (10574190), Munesh K. Harioudh (10574193), Neeraj K. Verma (4502554), Konica Porwal (9610847), Shivani Sharma (255210), Chirag Kulkarni (9610850), Amitabha Bandyopadhyay (67094), Madhav N. Mugale (10574196), Kalyan Mitra (514430), Jimut K. Ghosh (10574199), Naibedya Chattopadhyay (137586)

مصطلحات موضوعية: Biochemistry, Medicine, Pharmacology, Biotechnology, Ecology, Cancer, Hematology, Biological Sciences not elsewhere classified, support bone growth, 18- residue fragment, β- sheet structure, Human Lactoferrin Acts, Self-Assembling Nano-Globular Peptide, standard-of-care osteogenic peptide, 3 T 3 fibroblasts, LP 2

Relation: https://figshare.com/articles/journal_contribution/Self-Assembling_Nano-Globular_Peptide_from_Human_Lactoferrin_Acts_as_a_Systemic_Enhancer_of_Bone_Regeneration_A_Novel_Peptide_for_Orthopedic_Application/14390610

الاتاحة: https://doi.org/10.1021/acsami.1c01513.s001

المؤلفون: Yehong Gong (3643510), Chendi Zhan (4997939), Yu Zou (547570), Zhenyu Qian (1532839), Guanghong Wei (160915), Qingwen Zhang (294089)

مصطلحات موضوعية: Biophysics, Biochemistry, Cell Biology, Molecular Biology, Biotechnology, Immunology, Hematology, Computational Biology, Chemical Sciences not elsewhere classified, K 28 side chain, β- sheet structure, residue, Mel molecule exhibits, interaction, COO, MD, 500 ns all-atom, Ser, β 42 protofibril, Mel molecules, mechanism, AD

Relation: https://figshare.com/articles/journal_contribution/Serotonin_and_Melatonin_Show_Different_Modes_of_Action_on_A_sub_42_sub_Protofibril_Destabilization/13703202

الاتاحة: https://doi.org/10.1021/acschemneuro.1c00038.s001

المؤلفون: Mohsen Asadbegi (7486421), Amir Shamloo (3695023)

مصطلحات موضوعية: Biophysics, Biochemistry, Pharmacology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, β- sheet structure, zinc metal ion, multifunctional peptide, zinc metal ions, MD, zinc ion chelation, β 42 monomer, peptide chelating domain, Novel Computational Approach, β 42 aggregates, AD

Relation: https://figshare.com/articles/journal_contribution/Evaluating_the_Multifunctionality_of_a_New_Modulator_of_Zinc-Induced_A_Aggregation_Using_a_Novel_Computational_Approach/14079992

الاتاحة: https://doi.org/10.1021/acs.jcim.0c01264.s001

المؤلفون: Faraz Vosough (9998137), Andreas Barth (1922089)

مصطلحات موضوعية: Biophysics, Biochemistry, Neuroscience, Environmental Sciences not elsewhere classified, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, β42 oligomers, oligomer size, time-dependent band shift, β- sheet structure, time-resolved aggregation experiments, IR spectra, Oligomer Size Soluble oligomers, sodium dodecyl sulfate polyacrylami., Heterogeneous Amyloid -β42 Oligomer., time-resolved IR studies

Relation: https://figshare.com/articles/journal_contribution/Characterization_of_Homogeneous_and_Heterogeneous_Amyloid-_42_Oligomer_Preparations_with_Biochemical_Methods_and_Infrared_Spectroscopy_Reveals_a_Correlation_between_Infrared_Spectrum_and_Oligomer_Size/13602595

الاتاحة: https://doi.org/10.1021/acschemneuro.0c00642.s001

المؤلفون: Anon Thammasittirong, Chompounoot Imtong, Wilaiwan Sriwimol, Somsri Sakdee, Chanan Angsuthanasombat

المصدر: Toxins; Volume 11; Issue 2; Pages: 62

مصطلحات موضوعية: Cry4Ba toxin, C-terminal domain, membrane anchor, pore formation, proteinase K, β-sheet structure

جغرافية الموضوع: agris

وصف الملف: application/pdf

Relation: Bacterial Toxins; https://dx.doi.org/10.3390/toxins11020062

الاتاحة: https://doi.org/10.3390/toxins11020062

المؤلفون: Taiyo Yoshioka, Tsunenori Kameda

المصدر: The Journal of Silk Science and Technology of Japan. 2020, 28:127

المؤلفون: Roa Acosta, Diego Fernando, Hoyos Concha, José Luis, Bravo, Jesús Eduardo

المصدر: Biotecnología en el Sector Agropecuario y Agroindustrial: BSAA, ISSN 1692-3561, Vol. 20, Nº. 2 (Julio-diciembre), 2022, pags. 76-86

مصطلحات موضوعية: Firmness, Quinoa Protein, Rice protein, Soy protein, Hydrolysates, β-sheet structure, β-turns structure, Alcalase Enzyme, Flavorzime Enzyme, Infrared spectroscopy, Fourier transform, Firmeza, Proteína de Quinua, Proteína de Arroz, Proteína de Soya, Hidrolizados, Estructura β-sheet, estructura β-turns, Enzima Alcalasa, Enzima Flavorzima, Espectroscopia infrarroja, Función de Fourier

وصف الملف: application/pdf

Relation: https://dialnet.unirioja.es/servlet/oaiart?codigo=8505791; (Revista) ISSN 1909-9959; (Revista) ISSN 1692-3561

الاتاحة: https://dialnet.unirioja.es/servlet/oaiart?codigo=8505791

المؤلفون: Taiyo Yoshioka, Tsunenori Kameda

المصدر: The Journal of Silk Science and Technology of Japan. 2019, 27:95

المؤلفون: Libo Wang, Dale D.O. Martin, Erin Genter, Jianjun Wang, Roger S. McLeod, Donald M. Small

المصدر: Journal of Lipid Research, Vol 50, Iss 7, Pp 1340-1352 (2009)

مصطلحات موضوعية: adsorption, air/water interface, amphipathic β sheet structure, apoB, compressibility, desorption, Biochemistry, QD415-436

وصف الملف: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S0022227520307823; https://doaj.org/toc/0022-2275

URL الوصول: https://doaj.org/article/0b4faf0ffb52493288094db49aaefa35

المؤلفون: Murvai, Ünige, Somkuti, Judit, Smeller, László, Penke, Botond, Kellermayer, Miklós SZ

المصدر: Biochim Biophys Acta. , 1854(5), 327-32, (2015-01-17)

مصطلحات موضوعية: amyloid, atomic force microscopy, force spectroscopy, Fourier transform infrared spectroscopy, β-sheet structure, structural compaction

Relation: https://zenodo.org/communities/inmind; https://zenodo.org/communities/eu; https://doi.org/10.1016/j.bbapap.2015.01.003; oai:zenodo.org:48571

الاتاحة: https://doi.org/10.1016/j.bbapap.2015.01.003

المؤلفون: Solanas, Concepción, Torre, Beatriz G. de la, Fernández Reyes, María, Santiveri, Clara M., Jiménez, M. Ángeles, Rivas, Luis, Jiménez, Ana I., Andreu Martínez, David, Cativiela, Carlos

مصطلحات موضوعية: Gramidicin S, Cationic antimicrobial peptides, Phenylalanine analogs, NMR, β-turn, β-sheet structure

وصف الملف: application/pdf

Relation: Journal of Medicinal Chemistry. 2010; 53(10):4119-29; info:eu-repo/grantAgreement/ES/3PN/BIO2008-04487-CO3-0; http://hdl.handle.net/10230/36639; http://dx.doi.org/10.1021/jm100143f

الاتاحة: http://hdl.handle.net/10230/36639
https://doi.org/10.1021/jm100143f

المؤلفون: Kosuke Magami (10654473), Naomi Hachiya (3615488), Kazuo Morikawa (10654476), Noriko Fujii (153802), Takumi Takata (1694353)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Neuroscience, Pharmacology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, thioflavin T fluorescence, position 76. CD, amyloid-like fibrils, β- sheet structure, α A-crystallin-derived peptide, residue, 79A, 14 alanine substituents, 66 SDRDKFVIFLDVKHF 80, disassembling amyloid-like fibrils, PIMT, Asp, α A-crystallin-derived peptides, L-isoAsp, lens α A-crystallin

Relation: https://figshare.com/articles/figure/Comparison_of_the_secondary_structure_of_A66_80_L-isoAsp76_and_D76A_A66_80_peptides_/14425788

الاتاحة: https://doi.org/10.1371/journal.pone.0250277.s003

المؤلفون: Kosuke Magami (10654473), Naomi Hachiya (3615488), Kazuo Morikawa (10654476), Noriko Fujii (153802), Takumi Takata (1694353)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Neuroscience, Pharmacology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, thioflavin T fluorescence, position 76. CD, amyloid-like fibrils, β- sheet structure, α A-crystallin-derived peptide, residue, 79A, 14 alanine substituents, 66 SDRDKFVIFLDVKHF 80, disassembling amyloid-like fibrils, PIMT, Asp, α A-crystallin-derived peptides, L-isoAsp, lens α A-crystallin

Relation: https://figshare.com/articles/figure/LC-MS_chromatogram_of_the_A66_80_peptide_containing_L-isoAsp76_/14425782

الاتاحة: https://doi.org/10.1371/journal.pone.0250277.s001