Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study.
about
Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies.Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy.The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.Molecular dynamics of thermoenzymes at high temperature and pressure: a review.Some physico-chemical parameters that influence proteinase K resistance and the infectivity of PrPSc after high pressure treatment.
P2860
Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study.
description
2003 nî lūn-bûn
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
@zh-hk
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name
Pressure- and temperature-indu ...... m infrared spectroscopy study.
@en
type
label
Pressure- and temperature-indu ...... m infrared spectroscopy study.
@en
prefLabel
Pressure- and temperature-indu ...... m infrared spectroscopy study.
@en
P2093
P2860
P356
P1433
P1476
Pressure- and temperature-indu ...... m infrared spectroscopy study.
@en
P2093
Filip Meersman
Joost Haelewyn
Karel Heremans
Koen Goossens
Marc De Ley
P2860
P304
P356
10.1042/BJ20020717
P407
P577
2003-03-01T00:00:00Z