Single-Molecule Experiments Reveal the Flexibility of a Per-Arnt-Sim Domain and the Kinetic Partitioning in the Unfolding Pathway Under Force

Biophysical Journal - United States
doi 10.1016/j.bpj.2012.03.042
Full Text
Abstract

Available in full text

Categories
Biophysics
Date
Authors
Publisher

Elsevier BV

Related search

Novel Mutation in the Per-Arnt-Sim Domain of KCNH2 Causes a Malignant Form of Long-Qt Syndrome

Circulation
Cardiovascular MedicinePhysiologyCardiology
2005English

The Folding Pathway of a Fast-Folding Immunoglobulin Domain Revealed by Single-Molecule Mechanical Experiments

EMBO Reports
BiochemistryGeneticsMolecular Biology
2005English

Revealing the Bifurcation in the Unfolding Pathways of GFP by Using Single-Molecule Experiments and Simulations

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2007English

Optimizing the Calculation of Energy Landscape Parameters From Single-Molecule Protein Unfolding Experiments

Physical Review E
2015English

The E.coli Sec Pathway Under a Single-Molecule Loupe

Biophysical Journal
Biophysics
2016English

Reversible Unfolding and Folding of the Metalloprotein Ferredoxin Revealed by Single-Molecule Atomic Force Microscopy

Journal of the American Chemical Society
BiochemistryColloidCatalysisChemistrySurface Chemistry
2017English

Combined Single Molecule Force and Fluorescence Spectroscopy of the Unfolding and Refolding of Green Fluorescent Protein

Biophysical Journal
Biophysics
2014English

The Physics of Pulling Polyproteins: A Review of Single Molecule Force Spectroscopy Using the AFM to Study Protein Unfolding

Reports on Progress in Physics
MedicineAstronomyPhysics
2016English

Kinetic Ductility and Force-Spike Resistance of Proteins From Single-Molecule Force Spectroscopy

Biophysical Journal
Biophysics
2016English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy