The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins

Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

(2014) Jing Liu et al.   CHEMICAL REVIEWS

Copper Active Sites in Biology

(2014) Edward I. Solomon et al.   CHEMICAL REVIEWS

Protein co-translocational unfolding depends on the direction of pulling

(2014) David Rodriguez-Larrea et al.   Nature Communications

CHARMM36 all-atom additive protein force field: Validation based on comparison to NMR data

(2013) Jing Huang et al.   JOURNAL OF COMPUTATIONAL CHEMISTRY

Computational Study of the Structure and Electronic Circular Dichroism Spectroscopy of Blue Copper Proteins

(2013) Hainam Do et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Multiple Unfolding Pathways of Leucine Binding Protein (LBP) Probed by Single-Molecule Force Spectroscopy (SMFS)

(2013) Hema Chandra Kotamarthi et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Single Molecule Force Spectroscopy Reveals That Iron Is Released from the Active Site of Rubredoxin by a Stochastic Mechanism

(2013) Peng Zheng et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Multistep protein unfolding during nanopore translocation

(2013) David Rodriguez-Larrea et al.   Nature Nanotechnology

Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy

(2013) Ionel Popa et al.   Nature Protocols

Elasticity, structure, and relaxation of extended proteins under force

(2013) G. Stirnemann et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2012) Xiang Gao et al.   BIOPHYSICAL JOURNAL

Hydrogen Bond Strength Modulates the Mechanical Strength of Ferric-Thiolate Bonds in Rubredoxin

(2012) Peng Zheng et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Mechanically Untying a Protein Slipknot: Multiple Pathways Revealed by Force Spectroscopy and Steered Molecular Dynamics Simulations

(2012) Chengzhi He et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The Direction of Protein Entry into the Proteasome Determines the Variety of Products and Depends on the Force Needed to Unfold Its Two Termini

(2012) Dikla Berko et al.   MOLECULAR CELL

Direct Measurements of the Mechanical Stability of Zinc-Thiolate Bonds in Rubredoxin by Single-Molecule Atomic Force Microscopy

(2011) Peng Zheng et al.   BIOPHYSICAL JOURNAL

Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine

(2011) Marie-Eve Aubin-Tam et al.   CELL

ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates

(2011) Rodrigo A. Maillard et al.   CELL

Ligand-modulated Parallel Mechanical Unfolding Pathways of Maltose-binding Proteins

(2011) Vasudha Aggarwal et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Highly Covalent Ferric−Thiolate Bonds Exhibit Surprisingly Low Mechanical Stability

(2011) Peng Zheng et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Recent advances in understanding blue copper proteins

(2010) Edward I. Solomon et al.   COORDINATION CHEMISTRY REVIEWS

Understanding biology by stretching proteins: recent progress

(2010) Albert Galera-Prat et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Force-activated reactivity switch in a bimolecular chemical reaction

(2009) Sergi Garcia-Manyes et al.   Nature Chemistry

Mechanical Unfoldons as Building Blocks of Maltose-binding Protein

(2008) Morten Bertz et al.   JOURNAL OF MOLECULAR BIOLOGY

Spectroscopic and Density Functional Theory Studies of the Blue−Copper Site in M121SeM and C112SeC Azurin:  Cu−Se Versus Cu−S Bonding

(2008) Ritimukta Sarangi et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: Evidence for a kinetic partitioning mechanism

(2008) Q. Peng et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Apo-azurin folds via an intermediate that resembles the molten-globule

(2004) Anders Sandberg et al.   PROTEIN SCIENCE