Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding (Q22061732)

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

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English	Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding	scientific article	Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding

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

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Susan Marqusee

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Susan

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Marqusee

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Dimensions Publication ID

11 September 2022

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Chiwook Park

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Chiwook

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Park

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Dimensions Publication ID

11 September 2022

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publication date

17 February 2005

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2

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3

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207-212

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Mapping the transition state and pathway of protein folding by protein engineering

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Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants

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Propagation of a single destabilizing mutation throughout the Escherichia coli ribonuclease HI native state

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Calculation of protein extinction coefficients from amino acid sequence data

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Conformational stability of globular proteins

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Alternative packing arrangements in the hydrophobic core of λrepresser

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Structure and enzymatic break-down of proteins

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https://api.crossref.org/works/10.1038%2FNMETH740

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Induction of biological activity by limited proteolysis

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Experimental and Theoretical Aspects of Protein Folding

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Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1.

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Unfolding rates of globular proteins determined by kinetics of proteolysis

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Selecting proteins with improved stability by a phage-based method

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Probing the high energy states in proteins by proteolysis

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Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state

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Applications of thermolysin in protein structural analysis

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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A quantitative, high-throughput screen for protein stability

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A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution.

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Manipulation of ligand binding affinity by exploitation of conformational coupling

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Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein

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Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B.

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Quantitative protein stability measurement in vivo

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Electrophoretic analysis of the unfolding of proteins by urea

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7 January 2021

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Confirmation of the hierarchical folding of RNase H: a protein engineering study

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https://api.crossref.org/works/10.1038%2FNMETH740

7 January 2021

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Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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10.1038/NMETH740

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https://api.fatcat.wiki/v0/release/aib3irbxezcy7mzlpfvh4itwji

24 November 2022

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