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References from Second coordination sphere controls structural flexibility of blue copper protein: A basis for entatic state formation. Local targets link to admitted publications; unresolved targets remain external evidence.
Metalloproteins and metal sensing
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Rack-induced bonding in blue-copper proteins
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Recent advances in understanding blue copper proteins
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Electron transfers in chemistry and biology
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Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins
10.1021/cr0206317 · 2004 · External reference
Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy
10.1126/science.aam6203 · 2017 · External reference
Disabling the entatic control of methionine ligation through additive destabilization of ferric cytochrome c
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Fundamental properties of small molecule models of Fe-only hydrogenase: computations relative to the definition of an entatic state in the active site
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Medium- and short-chain dehydrogenase/reductase gene and protein families: the role of zinc for alcohol dehydrogenase structure and function
10.1007/s00018-008-8593-1 · 2008 · External reference
Zinc binding to peptide analogs of the structural zinc site in alcohol dehydrogenase: implications for an entatic state
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Structures of oxidized and reduced azurin II from alcaligenes xylosoxidans at 1.75 A resolution
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Structure of apo-azurin from Alcaligenes denitrificans at 1.8 A resolution
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The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide
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Flexibility of the metal-binding region in apo-cupredoxins
10.1073/pnas.1119460109 · 2012 · External reference
An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
10.1016/s0162-0134(02)00364-1 · 2002 · External reference
Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
10.1038/nature08551 · 2009 · External reference
Fifteen years of Raman spectroscopy of engineered Heme containing peroxidases: what have we learned?
10.1021/ar020112q · 2005 · External reference
The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis
10.1021/bi062139d · 2007 · External reference
Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures
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THE structure and unusual pH dependence of plastocyanin from the Fern Dryopteris crassirhizoma: THE PROTONATION OF AN ACTIVE SITE HISTIDINE IS HINDERED BY π-π INTERACTIONS
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The impact of second coordination sphere methionine-aromatic interactions in copper proteins
10.1021/acs.inorgchem.2c00030 · 2022 · External reference
Systematic elucidation of the second coordination sphere effect on the structure and properties of a blue copper protein, pseudoazurin
10.1016/j.jinorgbio.2023.112292 · 2023 · External reference
Non-covalent interactions in blue copper protein probed by Met16 mutation and electronic and resonance Raman spectroscopy of Achromobacter cycloclastes pseudoazurin
10.1016/j.jinorgbio.2009.11.004 · 2010 · External reference
Unresolved reference
2006 · External reference
Unresolved reference
2006 · External reference
Differential scanning calorimetry as a tool for protein folding and stability
10.1016/j.abb.2012.09.008 · 2013 · External reference
π–π interaction between aromatic ring and copper-coordinated His81 imidazole regulates the blue copper active-site structure
10.1007/s00775-006-0176-8 · 2007 · External reference
The influence of solvent composition on global dynamics of human butyrylcholinesterase powders: a neutron-scattering study
10.1016/s0006-3495(04)74363-5 · 2004 · External reference
EMU: high-resolution backscattering spectrometer at ANSTO
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How soft is a protein? A protein dynamics force constant measured by neutron scattering
10.1126/science.288.5471.1604 · 2000 · External reference
Protein dynamics: comparison of simulations with inelastic neutron scattering experiments
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Mantid—data analysis and visualization package for neutron scattering and μSR experiments
10.1016/j.nima.2014.07.029 · 2014 · External reference
A modern approach to QENS data analysis in mantid
10.1016/j.physb.2019.02.041 · 2019 · External reference
Picosecond to nanosecond dynamics provide a source of conformational entropy for protein folding
10.1039/c6cp04146a · 2016 · External reference
Unresolved reference
2006 · External reference
Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
10.1016/s0006-3495(00)76630-6 · 2000 · External reference
Deconvolution of complex differential scanning calorimetry profiles for protein transitions under kinetic control
10.1016/j.ab.2016.07.006 · 2016 · External reference
A benchmark for protein dynamics: ribonuclease a measured by neutron scattering in a large wavevector-energy transfer range
10.1016/j.chemphys.2007.09.012 · 2008 · External reference
Protein dynamics studied by neutron scattering
10.1017/s0033583502003840 · 2003 · External reference
Quasielastic neutron scattering in soft matter
10.1016/j.cocis.2009.04.002 · 2009 · External reference
Observation of fragile-to-strong dynamic crossover in protein hydration water
10.1073/pnas.0602474103 · 2006 · External reference
Macromolecular dynamics in red blood cells investigated using neutron spectroscopy
10.1098/rsif.2010.0306 · 2010 · External reference
Evolution of the internal dynamics of two globular proteins from dry powder to solution
10.1016/s0006-3495(99)76903-1 · 1999 · External reference
Dynamics of proteins with different molecular structures under solution condition
10.1038/s41598-020-78311-4 · 2020 · External reference
Data analysis of dynamics in protein solutions using quasi-elastic neutron scattering - important insights from polarized neutrons
2024 · External reference
Coherent structural relaxation of water from meso- to intermolecular scales measured using neutron spectroscopy with polarization analysis
10.1103/physrevresearch.2.022015 · 2020 · External reference
Impact of isotopic exchange on hydrated protein dynamics revealed by polarized neutron scattering
10.1103/prxlife.2.013005 · 2024 · External reference
A computational perspective to intermolecular interactionsand the role of the solvent on regulating protein properties
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Structural and genetic analysis of protein stability
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Protein stability, flexibility and function
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