المؤلفون: Jožica Dolenc (1858474), Esme J. Haywood (14301806), Tingting Zhu (334564), Lorna J. Smith (1931464)

مصطلحات موضوعية: Biophysics, Biochemistry, Molecular Biology, Pharmacology, Biotechnology, Cancer, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, Information Systems not elsewhere classified, unfolded extended chain, features help funnel, conformational insights provided, >)– co ­(<, preceding residue due, peptide remains folded, aminated peptide inhibitors, interstrand hydrogen bonding, aminated residues shows, bonding potential, aminated residues, aminated peptides, residue toward, residue involved, folded β, peptide starting, simulations shows, work give, sequence dependent, inhibit amyloid

Relation: https://figshare.com/articles/journal_contribution/Backbone_N_Amination_Promotes_the_Folding_of_Hairpin_Peptides_via_a_Network_of_Hydrogen_Bonds/21780440

الاتاحة: https://doi.org/10.1021/acs.jcim.2c00516.s001

المؤلفون: Qinsi Xiong (6481598), Samuel I. Stupp (1235823), George C. Schatz (1278267)

مصطلحات موضوعية: Biophysics, Biochemistry, Molecular Biology, Computational Biology, Biological Sciences not elsewhere classified, Information Systems not elsewhere classified, possible design rule, interstrand hydrogen bonds, assembled morphologies remains, assembled nanostructures including, ribbon twist angle, handed twisted ribbon, study provides insight, assembly morphology changes, flat ribbon, sheet twist, related morphology, molecular insight, suppressing right, suggesting arginine, sheet formation, sequence length, rgd epitope, relationship including, precisely predicting, potential use, peptide amphiphiles, insufficient understanding, handed β, grand challenge

Relation: https://figshare.com/articles/journal_contribution/Molecular_Insight_into_the_Sheet_Twist_and_Related_Morphology_of_Self-Assembled_Peptide_Amphiphile_Ribbons/16992055

الاتاحة: https://doi.org/10.1021/acs.jpclett.1c03243.s001

المؤلفون: Jasmin Spekowius (6689507), Rolf Pfister (2059357), Jan Helbing (1745620)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Molecular Biology, Sociology, Immunology, Mental Health, Infectious Diseases, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, UV, β- hairpin structures, stability, Conformation change, Trp residues, Tryptophan Zipper, transition, Thioamide Substitutions, thioamide ππ, time window, inward-pointing backbone carbonyls, interstrand hydrogen, unsubstituted sequence, AMPP photoswitch, thioamide subsitutions, tryptophan signal

Relation: https://figshare.com/articles/journal_contribution/Folding_and_Unfolding_of_the_Tryptophan_Zipper_in_the_Presence_of_Two_Thioamide_Substitutions/14923944

الاتاحة: https://doi.org/10.1021/acs.jpcb.1c03327.s001

المؤلفون: Jožica Dolenc (1858474), Esme J. Haywood (14301806), Tingting Zhu (334564), Lorna J. Smith (1931464)

مصطلحات موضوعية: Biophysics, Biochemistry, Molecular Biology, Pharmacology, Biotechnology, Cancer, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, Information Systems not elsewhere classified, unfolded extended chain, features help funnel, conformational insights provided, >)– co ­(<, preceding residue due, peptide remains folded, aminated peptide inhibitors, interstrand hydrogen bonding, aminated residues shows, bonding potential, aminated residues, aminated peptides, residue toward, residue involved, folded β, peptide starting, simulations shows, work give, sequence dependent, inhibit amyloid

Relation: https://figshare.com/articles/dataset/Backbone_N_Amination_Promotes_the_Folding_of_Hairpin_Peptides_via_a_Network_of_Hydrogen_Bonds/21780443

الاتاحة: https://doi.org/10.1021/acs.jcim.2c00516.s002