Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR. - Wikidata - wikimedia - TriplyDB

Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.

Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.

http://www.wikidata.org/entity/Q42845327

about

Thermostability of endo-1,4-beta-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS, hydrogen/deuterium-exchange reactions and dynamic light scattering Non-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins.Structural and kinetic characterization of the simplified SH3 domain FP1.Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein.Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry.The sequences of small proteins are not extensively optimized for rapid folding by natural selection.The hydrogen exchange core and protein folding.QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.Macromolecular crowding fails to fold a globular protein in cells Structural and kinetic mapping of side-chain exposure onto the protein energy landscape Adaptive local learning in sampling based motion planning for protein folding.Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.The calorimetric criterion for a two-state process revisited Scope and utility of hydrogen exchange as a tool for mapping landscapes Ruggedness in the folding landscape of protein L.The gramicidin dimer shows both EX1 and EX2 mechanisms of H/D exchange.Conformational changes in chemically modified Escherichia coli thioredoxin monitored by H/D exchange and electrospray ionization mass spectrometry.Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry.A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding.Molecular dynamics simulations of hydrophobic collapse of ubiquitin.Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure.Folding-unfolding energy change of a simple sphere model protein and an energy landscape of the folding process.

P2860

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P2860

Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.

http://www.wikidata.org/entity/Q42845327

description

1996 nî lūn-bûn

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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Direct evidence for a two-stat ...... e, mass spectrometry, and NMR.

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P2860

Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G

The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure

Primary structure effects on peptide group hydrogen exchange

Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange.

Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

A phage display system for studying the sequence determinants of protein folding

Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures.

Protein folding intermediates: native-state hydrogen exchange.

Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A.

Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G.

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1060-1066

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scholarly article

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10.1002/PRO.5560050608

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6

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8762137

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2143434

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