about
Optimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.When fast is better: protein folding fundamentals and mechanisms from ultrafast approachesPropensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolutionSingle Molecule Bioelectronics and Their Application to Amplification-Free Measurement of DNA Lengths.Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein.Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis.Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Proteins Breaking Bad: A Free Energy Perspective.Single molecule force spectroscopy at high data acquisition: A Bayesian nonparametric analysis.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Protein folding and unfolding under force
@ast
Protein folding and unfolding under force
@en
type
label
Protein folding and unfolding under force
@ast
Protein folding and unfolding under force
@en
prefLabel
Protein folding and unfolding under force
@ast
Protein folding and unfolding under force
@en
P2860
P356
P1433
P1476
Protein folding and unfolding under force
@en
P2093
Bharat Jagannathan
Susan Marqusee
P2860
P304
P356
10.1002/BIP.22321
P577
2013-11-01T00:00:00Z