Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.
about
Combining in Vitro and in Silico Single-Molecule Force Spectroscopy to Characterize and Tune Cellulosomal Scaffoldin Mechanics.Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry.Force-activated DNA substrates for probing individual proteins interacting with single-stranded DNA.Improved Free-Energy Landscape Quantification Illustrated with a Computationally Designed Protein-Ligand Interaction.A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy.FEATHER: Automated Analysis of Force Spectroscopy Unbinding and Unfolding Data via a Bayesian Algorithm
P2860
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P2860
Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年學術文章
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2017年學術文章
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name
Rapid Characterization of a Me ...... Site-Specific Bioconjugation.
@en
type
label
Rapid Characterization of a Me ...... Site-Specific Bioconjugation.
@en
prefLabel
Rapid Characterization of a Me ...... Site-Specific Bioconjugation.
@en
P2093
P2860
P50
P356
P1476
Rapid Characterization of a Me ...... Site-Specific Bioconjugation.
@en
P2093
Ayush Adhikari
David Rabuka
Devin T Edwards
Jacob A Greenberg
Marc-André LeBlanc
Ruby May A Sullan
Stephen R Okoniewski
William J Van Patten
P2860
P304
P356
10.1021/JACS.7B02958
P407
P577
2017-07-05T00:00:00Z