Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility.
about
Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues.Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.Ion-ion interactions in the denatured state contribute to the stabilization of CutA1 proteins.
P2860
Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility.
description
2014 nî lūn-bûn
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name
Thermodynamic analysis of unus ...... d its protease susceptibility.
@en
Thermodynamic analysis of unus ...... d its protease susceptibility.
@nl
type
label
Thermodynamic analysis of unus ...... d its protease susceptibility.
@en
Thermodynamic analysis of unus ...... d its protease susceptibility.
@nl
prefLabel
Thermodynamic analysis of unus ...... d its protease susceptibility.
@en
Thermodynamic analysis of unus ...... d its protease susceptibility.
@nl
P2093
P2860
P356
P1476
Thermodynamic analysis of unus ...... d its protease susceptibility.
@en
P2093
Bagautdin Bagautdinov
Etsuko Katoh
Hitoshi Yamamoto
Katsuhide Yutani
Kyoko Ogasahara
Masahide Sawano
Michiyo Takehira
Yoshinori Matsuura
P2860
P304
P356
10.1093/JB/MVU062
P50
P577
2014-10-24T00:00:00Z