about
Optimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.Unusually high mechanical stability of bacterial adhesin extender domains having calcium clampsTowards design principles for determining the mechanical stability of proteins.Nanomechanics of β-rich proteins related to neuronal disorders studied by AFM, all-atom and coarse-grained MD methods.Ca2+ binding enhanced mechanical stability of an archaeal crystallin.Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments.Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Binding of interferon reduces the force of unfolding for interferon receptor 1.The ribosomal protein Asc1/RACK1 is required for efficient translation of short mRNAsModular, Nondegenerate Polyprotein Scaffolds for Atomic Force Spectroscopy.Force spectroscopy studies on protein-ligand interactions: a single protein mechanics perspective.Probing interactions between human lung adenocarcinoma A549 cell and its aptamers at single-molecule resolution.The structure and function of cell membranes examined by atomic force microscopy and single-molecule force spectroscopy.Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2.Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers.Mechano-adaptive sensory mechanism of α-catenin under tension.Single-molecule studies on PolySUMO proteins reveal their mechanical flexibilitySingle-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.Multiple transitions between various ordered and disordered states of a helical polymer under stretching.Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building BlocksThe Role of Nanomechanics in Healthcare.On the non-stationary generalized Langevin equation.Sawtooth patterns in force-extension curves of biomolecules: an equilibrium-statistical-mechanics theory.Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Theory of force-extension curves for modular proteins and DNA hairpins.Tuning protein mechanics through an ionic cluster graft from an extremophilic protein.Spin variable approach for the statistical mechanics of folding and unfolding chains.Spectrometric-based techniques for metal-binding protein assessment in clinical, environmental, and food samples
P2860
Q27301025-1E427EAD-3635-44DD-9459-6DFAE9B9FD7CQ30400717-C9376B80-3AE0-4440-A661-B935075E7F43Q34976764-D649E9BA-A32F-4F35-9EE3-C3E3E627C1F3Q35100972-39A66FB9-5C02-46A2-A027-415ACD037737Q35146699-99E9E5EE-4F6B-4F94-9C4B-B6BC0CDE66C0Q35560688-44A76E1B-9DF5-455B-B4B5-FF50C5CCFF7AQ35608870-5DC01261-4E44-415F-9434-997684A9EC66Q36344846-F7F3DA76-8C4A-4CF4-971E-7003925BD7A3Q36844633-3281A808-3CCE-43CA-992E-4E0AEBD1842AQ37083477-4CA50BBA-D872-483A-9E11-4393B8D66297Q38205675-2FB1CDF3-405C-41A5-A34F-715E767189C7Q38303776-030D0E16-7C48-452A-B6E6-AE471891A949Q38429670-69D3CD6D-5519-42DE-A277-703C6C1E91B9Q38693432-419D4F20-9EBE-45C2-8898-1DD320C362EFQ39062760-FE6599D5-9AA6-498D-B4BB-72238DFAAB1AQ39221178-15357C07-7351-42F4-8F2F-3ED5BCE9DEBCQ39826471-3D3F60DA-A1FB-4084-9C13-A2D01F76EB9EQ40912791-BD237D17-6A8B-4259-BFCD-4DA2601D9DE0Q40949529-95212B69-57B8-4B3F-8148-CBCE09B46CBAQ41931069-C3DE9199-2DED-488B-A91F-7D8ECDD6D34AQ42316765-016B0B09-AAB2-45F4-8528-3676F0C90F63Q46250335-11F921D1-0717-43EB-8AEB-93FB5E489C5CQ47341899-AC760B02-FE71-4002-8231-F1998C1A8234Q47781011-63DEBFA8-88A8-49ED-9E06-419A59E0D4D6Q50879283-47BBF9C9-C8B5-4A87-8CF3-1BCF09F96177Q50900504-BDC81F3D-C6DB-4391-9419-838B4FA87A93Q51546845-7AF8B848-D5EF-48B1-8FFB-2B2A31AD29EEQ53550739-E7476CE4-BFB6-47DB-B189-7C18E0C15EACQ58389058-5E3EADE5-F046-4271-92A6-F9D2DEE5AB84
P2860
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Single molecule force spectroscopy using polyproteins.
@ast
Single molecule force spectroscopy using polyproteins.
@en
Single molecule force spectroscopy using polyproteins.
@en-gb
Single molecule force spectroscopy using polyproteins.
@nl
type
label
Single molecule force spectroscopy using polyproteins.
@ast
Single molecule force spectroscopy using polyproteins.
@en
Single molecule force spectroscopy using polyproteins.
@en-gb
Single molecule force spectroscopy using polyproteins.
@nl
prefLabel
Single molecule force spectroscopy using polyproteins.
@ast
Single molecule force spectroscopy using polyproteins.
@en
Single molecule force spectroscopy using polyproteins.
@en-gb
Single molecule force spectroscopy using polyproteins.
@nl
P2860
P356
P1476
Single molecule force spectroscopy using polyproteins.
@en
P2093
Toni Hoffmann
P2860
P304
P356
10.1039/C2CS35033E
P50
P577
2012-05-30T00:00:00Z