NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
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CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.Colorimetric and fluorometric monitoring of the helix composition of collagen-like peptides at the nM level.
P2860
NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.
description
2015 nî lūn-bûn
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2015年の論文
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name
NMR studies demonstrate a uniq ...... g a natural interruption site.
@ast
NMR studies demonstrate a uniq ...... g a natural interruption site.
@en
type
label
NMR studies demonstrate a uniq ...... g a natural interruption site.
@ast
NMR studies demonstrate a uniq ...... g a natural interruption site.
@en
prefLabel
NMR studies demonstrate a uniq ...... g a natural interruption site.
@ast
NMR studies demonstrate a uniq ...... g a natural interruption site.
@en
P2093
P2860
P356
P1476
NMR studies demonstrate a uniq ...... ng a natural interruption site
@en
P2093
Balaraman Madhan
Barbara Brodsky
Xiuxia Sun
P2860
P304
24201-24209
P356
10.1074/JBC.M115.654871
P407
P50
P577
2015-07-24T00:00:00Z