Lista de obras - Chiwook Park - Dominio Público Uruguay

A Cooperative Folding Unit as the Structural Link for Energetic Coupling within a Protein

artículo científico publicado en 2017

Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values

artículo científico publicado en 2004

Bacteriorhodopsin folds through a poorly organized transition state

artículo científico publicado en 2014

Catalysis by ribonuclease A is limited by the rate of substrate association

artículo científico publicado en 2003

Chaperone Action of a Cofactor in Protein Folding

scientific article published on 08 May 2020

Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin

artículo científico publicado en 2001

Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding

artículo científico publicado en 2001

Determining protein stability in cell lysates by pulse proteolysis and Western blotting

artículo científico publicado en 2009

Dimer formation by a "monomeric" protein

artículo científico publicado en 2000

Discovery of Nicotinamide Adenine Dinucleotide Binding Proteins in the Escherichia coli Proteome Using a Combined Energetic- and Structural-Bioinformatics-Based Approach.

artículo científico publicado en 2016

Effect of circular permutations on transient partial unfolding in proteins

artículo científico publicado en 2016

Energetic Coupling between Ligand Binding and Dimerization in Escherichia coli Phosphoglycerate Mutase

artículo científico publicado en 2016

Energetics-based discovery of protein-ligand interactions on a proteomic scale

artículo científico publicado en 2011

Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis

artículo científico publicado en 2007

Fast, Facile, Hypersensitive Assays for Ribonucleolytic Activity

article

Fluorescence assay for the binding of ribonuclease A to the ribonuclease inhibitor protein

artículo científico publicado en 2002

GalaxyHomomer: a web server for protein homo-oligomer structure prediction from a monomer sequence or structure

artículo científico publicado en 2017

His···Asp Catalytic Dyad of Ribonuclease A: Conformational Stability of the Wild-Type, D121N, D121A, and H119A Enzymes†

artículo científico publicado en 1998

Investigating protein unfolding kinetics by pulse proteolysis.

artículo científico publicado en 2009

Investigating the effect of temperature on transient partial unfolding by proteolysis.

artículo científico publicado en 2009

Ligand binding to a high-energy partially unfolded protein.

artículo científico publicado en 2014

Mapping transient partial unfolding by protein engineering and native-state proteolysis.

artículo científico publicado en 2009

Origin of the ‘inactivation’ of ribonuclease A at low salt concentration

scientific article published on 01 February 2000

Probing membrane protein unfolding with pulse proteolysis.

artículo científico publicado en 2010

Probing the high energy states in proteins by proteolysis

artículo científico publicado en 2004

Product inhibition in native-state proteolysis

artículo científico publicado en 2014

Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding

artículo científico publicado en 2005

Quantitative analysis of the effect of salt concentration on enzymatic catalysis.

artículo científico publicado en 2001

Quantitative determination of protein stability and ligand binding by pulse proteolysis

artículo científico publicado en 2006

Revisiting absorbance at 230nm as a protein unfolding probe

artículo científico publicado en 2009

Revisiting the folding kinetics of bacteriorhodopsin.

artículo científico publicado en 2011

Salt bridge as a gatekeeper against partial unfolding

artículo científico publicado en 2016

Selective stabilization of a partially unfolded protein by a metabolite.

artículo científico publicado en 2012

Simplified proteomics approach to discover protein-ligand interactions.

artículo científico publicado en 2012

Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway

artículo científico publicado en 2014

The Ribonucleolytic Activity of Angiogenin†

artículo científico publicado en 2002

Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state.

artículo científico publicado en 2011

Lista de obras de Chiwook Park

A Cooperative Folding Unit as the Structural Link for Energetic Coupling within a Protein

Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values

Bacteriorhodopsin folds through a poorly organized transition state

Catalysis by ribonuclease A is limited by the rate of substrate association

Chaperone Action of a Cofactor in Protein Folding

Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin

Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding

Determining protein stability in cell lysates by pulse proteolysis and Western blotting

Dimer formation by a "monomeric" protein

Discovery of Nicotinamide Adenine Dinucleotide Binding Proteins in the Escherichia coli Proteome Using a Combined Energetic- and Structural-Bioinformatics-Based Approach.

Effect of circular permutations on transient partial unfolding in proteins

Energetic Coupling between Ligand Binding and Dimerization in Escherichia coli Phosphoglycerate Mutase

Energetics-based discovery of protein-ligand interactions on a proteomic scale

Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis

Fast, Facile, Hypersensitive Assays for Ribonucleolytic Activity

Fluorescence assay for the binding of ribonuclease A to the ribonuclease inhibitor protein

GalaxyHomomer: a web server for protein homo-oligomer structure prediction from a monomer sequence or structure

His···Asp Catalytic Dyad of Ribonuclease A: Conformational Stability of the Wild-Type, D121N, D121A, and H119A Enzymes†

Investigating protein unfolding kinetics by pulse proteolysis.

Investigating the effect of temperature on transient partial unfolding by proteolysis.

Ligand binding to a high-energy partially unfolded protein.

Mapping transient partial unfolding by protein engineering and native-state proteolysis.

Origin of the ‘inactivation’ of ribonuclease A at low salt concentration

Probing membrane protein unfolding with pulse proteolysis.

Probing the high energy states in proteins by proteolysis

Product inhibition in native-state proteolysis

Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding

Quantitative analysis of the effect of salt concentration on enzymatic catalysis.

Quantitative determination of protein stability and ligand binding by pulse proteolysis

Revisiting absorbance at 230nm as a protein unfolding probe

Revisiting the folding kinetics of bacteriorhodopsin.

Salt bridge as a gatekeeper against partial unfolding

Selective stabilization of a partially unfolded protein by a metabolite.

Simplified proteomics approach to discover protein-ligand interactions.

Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway

The Ribonucleolytic Activity of Angiogenin†

Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state.