Temperature-induced conformational switch in intestinal fatty acid binding protein (IFABP) revealing an alternative mode for ligand binding.
about
Structural coalescence underlies the aggregation propensity of a β-barrel protein motifTruncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation.Dissection of a beta-barrel motif leads to a functional dimer: the case of the intestinal fatty acid binding protein.Delta98Delta, a minimalist model of antiparallel beta-sheet proteins based on intestinal fatty acid binding proteinThe interaction of lipophilic drugs with intestinal fatty acid-binding protein.Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.Tethered domains and flexible regions in tRNase Z(L), the long form of tRNase Z.Frequency-control of protein translocation across an oscillating nanopore.
P2860
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P2860
Temperature-induced conformational switch in intestinal fatty acid binding protein (IFABP) revealing an alternative mode for ligand binding.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Temperature-induced conformati ...... ative mode for ligand binding.
@ast
Temperature-induced conformati ...... ative mode for ligand binding.
@en
type
label
Temperature-induced conformati ...... ative mode for ligand binding.
@ast
Temperature-induced conformati ...... ative mode for ligand binding.
@en
prefLabel
Temperature-induced conformati ...... ative mode for ligand binding.
@ast
Temperature-induced conformati ...... ative mode for ligand binding.
@en
P356
P1433
P1476
Temperature-induced conformati ...... ative mode for ligand binding.
@en
P2093
José M Delfino
P304
P356
10.1021/BI020680D
P407
P577
2003-06-01T00:00:00Z