Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.
about
StaRProtein, a web server for prediction of the stability of repeat proteins.Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks.A method for rapid high-throughput biophysical analysis of proteins.LcrH, a class II chaperone from the type three secretion system, has a highly flexible native structureIsing Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Investigation of effects of terpene skin penetration enhancers on stability and biological activity of lysozyme.Removal of a consensus proline is not sufficient to allow tetratricopeptide repeat oligomerization.Fibrous Nanostructures from the Self-Assembly of Designed Repeat Protein ModulesIntermediates in the folding equilibrium of repeat proteins from the TPR family
P2860
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P2860
Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Modulation of the multistate f ...... trinsic and extrinsic factors.
@en
Modulation of the multistate f ...... trinsic and extrinsic factors.
@nl
type
label
Modulation of the multistate f ...... trinsic and extrinsic factors.
@en
Modulation of the multistate f ...... trinsic and extrinsic factors.
@nl
prefLabel
Modulation of the multistate f ...... trinsic and extrinsic factors.
@en
Modulation of the multistate f ...... trinsic and extrinsic factors.
@nl
P2093
P2860
P356
P1433
P1476
Modulation of the multistate f ...... ntrinsic and extrinsic factors
@en
P2093
C Millership
E R G Main
P2860
P304
P356
10.1002/PRO.2018
P577
2012-03-01T00:00:00Z