Mechanism of phage P22 tailspike protein folding mutations.
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Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a MyovirusBacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linkerRole for cysteine residues in the in vivo folding and assembly of the phage P22 tailspikeInclusion body formation by interleukin-1 beta depends on the thermal sensitivity of a folding intermediate.Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspikeThe interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationPhage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.Sequence-specific recognition of DNA by hydrophobic, alanine-rich mutants of the basic region/leucine zipper motif investigated by fluorescence anisotropy.Three amino acids that are critical to formation and stability of the P22 tailspike trimer.C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.Connection between gene dosage and protein stability revealed by a high-yield production of recombinant proteins in an E. coli LexA1(Ind-) background.A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone.
P2860
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P2860
Mechanism of phage P22 tailspike protein folding mutations.
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Mechanism of phage P22 tailspike protein folding mutations.
@ast
Mechanism of phage P22 tailspike protein folding mutations.
@en
Mechanism of phage P22 tailspike protein folding mutations.
@nl
type
label
Mechanism of phage P22 tailspike protein folding mutations.
@ast
Mechanism of phage P22 tailspike protein folding mutations.
@en
Mechanism of phage P22 tailspike protein folding mutations.
@nl
prefLabel
Mechanism of phage P22 tailspike protein folding mutations.
@ast
Mechanism of phage P22 tailspike protein folding mutations.
@en
Mechanism of phage P22 tailspike protein folding mutations.
@nl
P2860
P356
P1433
P1476
Mechanism of phage P22 tailspike protein folding mutations.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560021109
P577
1993-11-01T00:00:00Z