Protein crowder charge and protein stability.

PubWeight™: 0.91‹?›

🔗 View Article (PMID 24552162)

Published in Biochemistry on March 03, 2014

Authors

Mohona Sarkar1, Joe Lu, Gary J Pielak

Author Affiliations

1: Department of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599-3290, United States.

Articles by these authors

FlgM gains structure in living cells. Proc Natl Acad Sci U S A (2002) 2.46

Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder. J Mol Biol (2005) 2.01

Effects of proteins on protein diffusion. J Am Chem Soc (2010) 1.58

Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy. J Am Chem Soc (2008) 1.49

Protein crowding tunes protein stability. J Am Chem Soc (2011) 1.49

Protein (19)F NMR in Escherichia coli. J Am Chem Soc (2010) 1.46

Impact of protein denaturants and stabilizers on water structure. J Am Chem Soc (2004) 1.39

Macromolecular crowding and protein stability. J Am Chem Soc (2012) 1.38

The cellular environment stabilizes adenine riboswitch RNA structure. Biochemistry (2013) 1.38

Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry (2010) 1.37

Residue-level interrogation of macromolecular crowding effects on protein stability. J Am Chem Soc (2008) 1.33

Macromolecular crowding fails to fold a globular protein in cells. J Am Chem Soc (2011) 1.21

Impact of reconstituted cytosol on protein stability. Proc Natl Acad Sci U S A (2013) 1.20

Unexpected effects of macromolecular crowding on protein stability. Biochemistry (2012) 1.17

Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein. Protein Sci (2006) 1.14

In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR. J Am Chem Soc (2011) 1.11

Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry (2003) 1.10

Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev (2014) 1.10

Retracted Protein dynamics in living cells. Biochemistry (2005) 1.10

Stability and apoptotic activity of recombinant human cytochrome c. Biochem Biophys Res Commun (2003) 1.06

Translational and rotational diffusion of a small globular protein under crowded conditions. J Phys Chem B (2009) 1.05

19F NMR studies of alpha-synuclein conformation and fibrillation. Biochemistry (2009) 1.04

Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions. J Am Chem Soc (2009) 1.02

Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli. Biochemistry (2009) 0.98

19F NMR studies of α-synuclein-membrane interactions. Protein Sci (2010) 0.97

Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. Chembiochem (2010) 0.94

In-cell protein NMR and protein leakage. Proteins (2011) 0.93

Interaction of α-synuclein with vesicles that mimic mitochondrial membranes. Biochim Biophys Acta (2011) 0.93

High-precision, high-throughput stability determinations facilitated by robotics and a semiautomated titrating fluorometer. Biochemistry (2003) 0.92

Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability. Methods Enzymol (2009) 0.91

Retraction. Biochemistry (2007) 0.91

Quantifying green fluorescent protein diffusion in Escherichia coli by using continuous photobleaching with evanescent illumination. J Phys Chem B (2009) 0.90

(19) F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells. Chemistry (2013) 0.88

Peeking into living eukaryotic cells with high-resolution NMR. Proc Natl Acad Sci U S A (2006) 0.88

Amide proton exchange of a dynamic loop in cell extracts. Protein Sci (2013) 0.87

A bioreactor for in-cell protein NMR. J Magn Reson (2009) 0.86

Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation. Biochemistry (2008) 0.86

Searching for quantitative entropy-enthalpy compensation among protein variants. Proteins (2002) 0.86

Probing the micelle-bound aggregation-prone state of α-synuclein with (19)F NMR spectroscopy. Chembiochem (2010) 0.85

Hydrogen exchange of disordered proteins in Escherichia coli. Protein Sci (2015) 0.85

Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerization. Protein Sci (2002) 0.83

Retracted Cytosol has a small effect on protein backbone dynamics. Biochemistry (2006) 0.82

Peroxidative aggregation of alpha-synuclein requires tyrosines. Protein Sci (2004) 0.82

Disordered Protein Diffusion under Crowded Conditions. J Phys Chem Lett (2012) 0.82

Development and cardiac contractility: cardiac troponin T isoforms and cytosolic calcium in rabbit. Pediatr Res (2006) 0.79

An upper limit for macromolecular crowding effects. BMC Biophys (2011) 0.79

Reconsideration of sedimentation equilibrium distributions reflecting the effects of small inert cosolutes on the dimerization of alpha-chymotrypsin. Biophys Chem (2007) 0.78

Crowding by trisaccharides and the 2:1 cytochrome c-cytochrome c peroxidase complex. Biochemistry (2002) 0.78

Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by ¹⁹F NMR. Mol Pharm (2012) 0.78

Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modeling. Biochemistry (2003) 0.78

An osmolyte mitigates the destabilizing effect of protein crowding. Protein Sci (2014) 0.76

Strategies for protein NMR in Escherichia coli. Biochemistry (2014) 0.76

Pressure perturbation calorimetry of helical peptides. Proteins (2006) 0.76

Cosolutes, Crowding and Protein Folding Kinetics. J Phys Chem B (2017) 0.75