Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin.
about
Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies.Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin.Pressure and temperature stability of the main apple allergen Mal d1.Cold instability of aponeocarzinostatin and its stabilization by labile chromophore.Deciphering structural intermediates and genotoxic fibrillar aggregates of albumins: a molecular mechanism underlying for degenerative diseases.Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressureDissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.The role of the 132-160 region in prion protein conformational transitions.Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.Variation in structure of proteins by adjusting reactive oxygen and nitrogen species generated from dielectric barrier discharge jet.Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS)Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study.Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.Sonication of proteins causes formation of aggregates that resemble amyloid.Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopyHigh-pressure studies of aggregation of recombinant human interleukin-1 receptor antagonist: thermodynamics, kinetics, and application to accelerated formulation studies.Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding.Increased susceptibility of beta-glucosidase from the hyperthermophile Pyrococcus furiosus to thermal inactivation at higher pressures.Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry.Effect of high pressure treatment on the color of fresh and processed meats: A review.The effect of the buffer solution on the adsorption and stability of horse heart myoglobin on commercial mesoporous titanium dioxide: a matter of the right choice.Enzymes from piezophiles.The unfolding effects on the protein hydration shell and partial molar volume: a computational study.Effect of high pressure processing on dispersive and aggregative properties of almond milk.Characterization of recombinant human granulocyte colony-stimulating factor expression by FT-IR spectroscopy: Studies on thermal induction and media formulation on the stability of the protein secondary structure.Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy.Probing conformational and functional substates of calmodulin by high pressure FTIR spectroscopy: influence of Ca2+ binding and the hypervariable region of K-Ras4B.Extraordinary stability of hemocyanins from L. polyphemus and E. californicum studied using infrared spectroscopy from 294 to 20 K.Application of ATR-FTIR spectroscopy to the study of thermally induced changes in secondary structure of protein molecules in solid state.Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding e
P2860
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P2860
Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Comparative Fourier transform ...... and aggregation of myoglobin.
@en
type
label
Comparative Fourier transform ...... and aggregation of myoglobin.
@en
prefLabel
Comparative Fourier transform ...... and aggregation of myoglobin.
@en
P2093
P2860
P1433
P1476
Comparative Fourier transform ...... and aggregation of myoglobin.
@en
P2093
Filip Meersman
Karel Heremans
László Smeller
P2860
P304
P356
10.1016/S0006-3495(02)75605-1
P407
P577
2002-05-01T00:00:00Z