Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.
about
Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: relative stabilities in experiment and simulationsProtein folding and function: the N-terminal fragment in adenylate kinase.Reducing the computational complexity of protein folding via fragment folding and assemblyStructured disorder and conformational selection.Folding/unfolding/refolding of proteins: present methodologies in comparison with capillary zone electrophoresis.Anatomy of protein structures: visualizing how a one-dimensional protein chain folds into a three-dimensional shape.Conformational equilibria and rates of localized motion within hepatitis B virus capsidsOctapeptide repeat insertions increase the rate of protease-resistant prion protein formationComparison of protein fragments identified by limited proteolysis and by computational cutting of proteins.Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysisThermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).Topological investigation of amyloid fibrils obtained from beta2-microglobulin.Characterization and identification of a chymotryptic hydrolysate of alpha-lactalbumin stimulating cholecystokinin release in STC-1 cells.An N-terminal domain of herpes simplex virus type Ig E is capable of forming stable complexes with gI.A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability.Stepwise proteolytic removal of the beta subdomain in alpha-lactalbumin. The protein remains folded and can form the molten globule in acid solution.Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis.Behaviour of oleic acid-depleted bovine alpha-lactalbumin made LEthal to tumor cells (BAMLET).The oleic acid complexes of proteolytic fragments of α-lactalbumin display apoptotic activity
P2860
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P2860
Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Limited proteolysis of bovine ...... terization of protein domains.
@ast
Limited proteolysis of bovine ...... terization of protein domains.
@en
type
label
Limited proteolysis of bovine ...... terization of protein domains.
@ast
Limited proteolysis of bovine ...... terization of protein domains.
@en
prefLabel
Limited proteolysis of bovine ...... terization of protein domains.
@ast
Limited proteolysis of bovine ...... terization of protein domains.
@en
P2093
P2860
P356
P1433
P1476
Limited proteolysis of bovine ...... terization of protein domains.
@en
P2093
De Filippis V
Polverino de Laureto P
Scaramella E
Wondrich FG
Zambonin M
P2860
P304
P356
10.1110/PS.8.11.2290
P577
1999-11-01T00:00:00Z