scholarly article | Q13442814 |
P2093 | author name string | Erik J Fernandez | |
Scott A Tobler | |||
P2860 | cites work | A nuclear magnetic resonance study of the hydrogen-exchange behaviour of lysozyme in crystals and solution | Q57889980 |
Determination of amide hydrogen exchange rates in peptides by mass spectrometry | Q67967266 | ||
Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers | Q69357373 | ||
Relative effectiveness of various ions on the solubility and crystal growth of lysozyme | Q69936625 | ||
Structural studies on acid unfolding and refolding of recombinant human interferon gamma | Q69980734 | ||
Evidence for a self-associating equilibrium intermediate during folding of human growth hormone | Q70557008 | ||
Protein stability parameters measured by hydrogen exchange | Q72416539 | ||
Amyloidosis | Q72573267 | ||
Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry | Q73285512 | ||
Identification of unfolding domains in large proteins by their unfolding rates | Q74510998 | ||
Aggregation of recombinant human interferon gamma: kinetics and structural transitions | Q77182872 | ||
Defining protein ensembles with native-state NH exchange: kinetics of interconversion and cooperative units from combined NMR and MS analysis | Q77789714 | ||
Thermal denaturation of human gamma-interferon. A calorimetric and spectroscopic study | Q77937502 | ||
Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics | Q78104493 | ||
Circular dichroism study of NaSCN effect on conformation of poly-L-lysine | Q93660444 | ||
Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation | Q24675910 | ||
Three-dimensional structure of recombinant human interferon-gamma | Q27652972 | ||
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis | Q27734827 | ||
Hydrogen exchange and structural dynamics of proteins and nucleic acids | Q28262950 | ||
Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor | Q28293731 | ||
Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin | Q28306450 | ||
Primary structure effects on peptide group hydrogen exchange | Q29614750 | ||
Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 beta point mutant modified in a surface loop | Q30194829 | ||
Probing residue-level unfolding during lysozyme precipitation | Q30303684 | ||
Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry | Q30307191 | ||
Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry | Q30426931 | ||
Hydrogen exchange: the modern legacy of Linderstrøm-Lang | Q30427220 | ||
Ligand binding to proteins: the binding landscape model | Q30428684 | ||
Detection of transient protein folding populations by mass spectrometry | Q34344353 | ||
Protein aggregation: folding aggregates, inclusion bodies and amyloid | Q34460420 | ||
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. | Q36199183 | ||
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR. | Q36280411 | ||
A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma | Q36730176 | ||
Disulfide bonds and thermal stability in T4 lysozyme | Q37482312 | ||
Protein stability: electrostatics and compact denatured states | Q37510917 | ||
Hydrogen Exchange in Proteins | Q40040717 | ||
Mutations and off-pathway aggregation of proteins | Q40534798 | ||
The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation. | Q40723588 | ||
Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea | Q40734460 | ||
Touring the landscapes: partially folded proteins examined by hydrogen exchange | Q41566813 | ||
The molecular basis of amyloidosis. | Q41691957 | ||
Aggregation and denaturation of apomyoglobin in aqueous urea solutions | Q43812801 | ||
Engineered disulfide bonds in recombinant human interferon-gamma: the impact of the N-terminal helix A and the AB-loop on protein stability | Q44250434 | ||
pH dependence of the reversible and irreversible thermal denaturation of gamma interferons | Q44716350 | ||
The effect of benzyl alcohol on recombinant human interferon-gamma | Q46186532 | ||
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin | Q46929622 | ||
Protein-protein interactions as a means of purification | Q47847135 | ||
Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition | Q47960195 | ||
Preferential interactions of proteins with salts in concentrated solutions. | Q52712617 | ||
Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma | Q57080267 | ||
P433 | issue | 6 | |
P304 | page(s) | 1340-1352 | |
P577 | publication date | 2002-06-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | Structural features of interferon-gamma aggregation revealed by hydrogen exchange | |
P478 | volume | 11 |
Q35223810 | Advances and challenges in analytical characterization of biotechnology products: mass spectrometry-based approaches to study properties and behavior of protein therapeutics |
Q30430967 | Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography |
Q36559830 | Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils |
Q38110611 | High-resolution MS for structural characterization of protein therapeutics: advances and future directions |
Q40275480 | Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin |
Q49739130 | Recombinant IFN-γ from the bank vole Myodes glareolus: a novel tool for research on rodent reservoirs of zoonotic pathogens |
Q30438164 | Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis |
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