Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine.
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Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different proteaseThe conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroniFine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antiterminationThe prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityStructural and energetic basis of infection by the filamentous bacteriophage IKeThe 1.5-A resolution crystal structure of bacterial luciferase in low salt conditionsA partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited foldingExtremely rapid protein folding in the absence of intermediates.Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule.Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.On the non-respect of the thermodynamic cycle by DsbA variants.A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.The crystal structure of the cis-proline to glycine variant (P114G) of ribonuclease A.Role of the Cys 2-Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1.Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation.Structural rearrangements on HIV-1 Tat (32-72) TAR complex formation.The role of a trans-proline in the folding mechanism of ribonuclease T1.
P2860
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P2860
Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@en
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@nl
type
label
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@en
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@nl
prefLabel
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@en
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@nl
P2093
P356
P1476
Stability and folding kinetics ...... f cis-proline 39 with alanine.
@en
P2093
P304
P356
10.1006/JMBI.1993.1336
P407
P577
1993-06-01T00:00:00Z