Effect of self-association on the structural organization of partially folded proteins: inactivated actin.

Effect of self-association on the structural organization of partially folded proteins: inactivated actin.

Item
http://www.wikidata.org/entity/Q40153494
Detection and characterization of partially unfolded oligomers of the SH3 domain of alpha-spectrin.The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT.Thermal unfolding and aggregation of actin.Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Native globular actin has a thermodynamically unstable quasi-stationary structure with elements of intrinsic disorder.Specific cleavage of the DNase-I binding loop dramatically decreases the thermal stability of actin.Denatured collapsed states in protein folding: example of apomyoglobin.The effect of PAMAM dendrimers on human and bovine serum albumin at different pH and NaCl concentrations.
P2860

Effect of self-association on the structural organization of partially folded proteins: inactivated actin.

Item
http://www.wikidata.org/entity/Q40153494
description
1999 nî lūn-bûn
@nan
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
1999年论文
@zh
1999年论文
@zh-cn
name
Effect of self-association on ...... d proteins: inactivated actin.
@en
type
label
Effect of self-association on ...... d proteins: inactivated actin.
@en
prefLabel
Effect of self-association on ...... d proteins: inactivated actin.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
Effect of self-association on ...... d proteins: inactivated actin.
@en
P2093
P2860
P304
P31
P356
10.1016/S0006-3495(99)77111-0
P407
P433
P478
P577
P698
P921
P932