Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity
about
Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a MyovirusBacteriophage SP6 is closely related to phages K1-5, K5, and K1E but encodes a tail protein very similar to that of the distantly related P22.On human disease-causing amino acid variants: statistical study of sequence and structural patterns.Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.
P2860
Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mutations improving the foldin ...... its receptor binding activity
@ast
Mutations improving the foldin ...... its receptor binding activity
@en
Mutations improving the foldin ...... its receptor binding activity
@nl
type
label
Mutations improving the foldin ...... its receptor binding activity
@ast
Mutations improving the foldin ...... its receptor binding activity
@en
Mutations improving the foldin ...... its receptor binding activity
@nl
prefLabel
Mutations improving the foldin ...... its receptor binding activity
@ast
Mutations improving the foldin ...... its receptor binding activity
@en
Mutations improving the foldin ...... its receptor binding activity
@nl
P2093
P356
P1476
Mutations improving the foldin ...... its receptor binding activity
@en
P2093
P304
P356
10.1006/JMBI.1999.3165
P407
P577
1999-10-01T00:00:00Z