Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
about
The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homologThe Exquisite Structure and Reaction Mechanism of Bacterial Pz-peptidase A toward Collagenous Peptides: X-RAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS OF PZ-PEPTIDASE A REVEALS DIFFERENCES FROM MAMMALIAN THIMET OLIGOPEPTIDASEA Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature ActivityMutational and Structural Analysis of L-N-Carbamoylase Reveals New Insights into a Peptidase M20/M25/M40 Family MemberDetermination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplingsEdge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseProtein dynamism and evolvability.Coping with thermal challenges: physiological adaptations to environmental temperatures.Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles.Biological function in a non-native partially folded state of a proteinStabilization of a protein conferred by an increase in folded state entropyIntrinsically semi-disordered state and its role in induced folding and protein aggregation"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.A hydrolase from Lactobacillus sakei moonlights as a transaminase.Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates.Characterizing intermolecular interactions that initiate native-like protein aggregation.Mechanical unfolding of acylphosphatase studied by single-molecule force spectroscopy and MD simulations.The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.
P2860
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P2860
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@en
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@nl
type
label
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@en
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@nl
prefLabel
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@en
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@nl
P2093
P50
P356
P1433
P1476
Structure, conformational stab ...... phile Sulfolobus solfataricus.
@en
P2093
Cristina Capanni
Fabrizio Chiti
Gennaro Esposito
Georgia Plakoutsi
Katiuscia Pagano
Paolo Viglino
Simone Zuccotti
Vera Alverdi
P2860
P356
10.1002/PROT.20703
P407
P577
2006-01-01T00:00:00Z