Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.
about
Circular permutation of 5-aminolevulinate synthase. Mapping the polypeptide chain to its functionRandom circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and functionTesting the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded formsA decade and a half of protein intrinsic disorder: biology still waits for physicsProduction of cyclic peptides and proteins in vivoA test of the relationship between sequence and structure in proteins: excision of the heme binding site in apocytochrome b5.A transposase strategy for creating libraries of circularly permuted proteins.Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthaseComparative laboratory evolution of ordered and disordered enzymes.Human topoisomerase I C-terminal domain fragment containing the active site tyrosine is a molten globule: implication for the formation of competent productive complex.Increased phospholipase A2 activity with phosphorylation of peroxiredoxin 6 requires a conformational change in the protein.Evolution of the folding ability of proteins through functional selectionIn vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.Biological function in a non-native partially folded state of a proteinAn enzymatic molten globule: efficient coupling of folding and catalysis.Protein phosphorylation corrects the folding defect of the neuroblastoma (S120G) mutant of human nucleoside diphosphate kinase A/Nm23-H1.Reversible thermal denaturation of a 60-kDa genetically engineered beta-sheet polypeptide.Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling.A generic hierarchical screening method for the analysis of microscale refolds using an automated robotic platform.Botulinum neurotoxin: unique folding of enzyme domain of the most-poisonous poison.Mechanism of salt-induced activity enhancement of a marine-derived laccase, Lac15.Denatured collapsed states in protein folding: example of apomyoglobin.S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin.Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme
P2860
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P2860
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Circularly permuted dihydrofol ...... interaction with its ligands.
@ast
Circularly permuted dihydrofol ...... interaction with its ligands.
@en
type
label
Circularly permuted dihydrofol ...... interaction with its ligands.
@ast
Circularly permuted dihydrofol ...... interaction with its ligands.
@en
prefLabel
Circularly permuted dihydrofol ...... interaction with its ligands.
@ast
Circularly permuted dihydrofol ...... interaction with its ligands.
@en
P2093
P2860
P356
P1433
P1476
Circularly permuted dihydrofol ...... y interaction with its ligands
@en
P2093
Kutyshenko VP
Protasova NYu
Uversky VN
Vassilenko KS
P2860
P304
P356
10.1002/PRO.5560050910
P577
1996-09-01T00:00:00Z