Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A.
about
The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteinsMolecular confinement influences protein structure and enhances thermal protein stabilityIn vitro membrane-inserted conformation of the cytochrome b(5) tailTruncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation.Conformational changes of alpha-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study.Protein stability modulated by a conformational effector: effects of trifluoroethanol on bovine serum albumin.Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation.Experimental validation of the role of trifluoroethanol as a nanocrowder.Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome cJuxtanodin is an intrinsically disordered F-actin-binding protein.Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins.Alpha-helix formation in melittin and beta-lactoglobulin A induced by fluorinated dialcoholsComparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered.Study of cosolvent-induced alpha-chymotrypsin fibrillogenesis: does protein surface hydrophobicity trigger early stages of aggregation reaction?Conformational intermediate of the amyloidogenic protein beta 2-microglobulin at neutral pH.Activity and conformational changes of horseradish peroxidase in trifluoroethanol.Dissecting the effect of trifluoroethanol on ribonuclease A. Subtle structural changes detected by nonspecific proteases.Secondary-structure analysis of alcohol-denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy.Inactivation and conformational changes of creatine kinase at low concentrations of hexafluoroisopropanol solutions.Interactions of trifluroethanol with the Trp-cage peptide.Hydrophobic fluorine mediated switching of the hydrogen bonding site as well as orientation of water molecules in the aqueous mixture of monofluoroethanol: IR, molecular dynamics and quantum chemical studies.Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes.Structural properties of apolipoprotein A-I mimetic peptides that promote ABCA1-dependent cholesterol efflux.Structural Characterization of the Intrinsically Disordered Protein p53 Using Raman Spectroscopy.A new bioproduction route for a novel antimicrobial peptide.
P2860
Q24533570-6440A245-0AD1-471C-86C7-7BAEE516F9F9Q28361355-720555ED-BC38-4280-9F65-A1DBDBD94793Q28594573-4F260587-05A3-4542-AE09-CDC2C01D9A22Q30155170-4C14122B-FF7D-4D90-9652-7BE37B9C32FFQ30370957-DC78984C-9C0E-4E8F-AFA2-2B3AEDD6512AQ30377047-BF4A8212-9467-4DF5-ABE7-F7F8BE3E168FQ31067429-5FF57901-2C8A-4893-BE2A-A18EA1844376Q34281435-27972D13-192C-43B3-A21A-98B5AD62C507Q36281928-3E5DFB3C-2683-45F8-9DFC-8CDF1E49BAB9Q36431740-363A92B4-18B8-4D71-A798-75B6630C0666Q36639468-197B1607-FB8B-432C-83AC-CF4E70B14EC1Q36965898-D12B9C46-721D-4DC4-97D9-47F0DC6B3C84Q38190250-71FA2C7C-10DD-4285-92F5-6AF3F170E40FQ40973048-CEE832C8-ACFA-41B6-8FDC-71B31617C863Q43273763-CC665466-8C3C-4536-8858-ACF5470D98AFQ43648155-A6827A15-F93F-4837-8B8C-16378AF736C3Q43979202-19EB682B-37A6-428D-B24A-2002BB0A5A70Q44086603-2BC62E2B-FD8E-463B-9EB2-87E9995A3902Q44245143-4E1CF62E-F3A1-4298-8B85-AA4948C1F3D0Q44625557-BB4341E7-C8B2-4A16-9877-0D1DE07DA0CFQ46679837-286000C9-FC70-4F2A-99AF-DF2D0CE025CFQ47907611-ADFEB56D-92D6-4F0B-9ED6-6376C1602696Q47985099-28F28B30-9018-41DD-A33F-F8635FA1C826Q47988665-D67BF604-8C13-41CD-9E12-3ECE8A34F7E3Q49309273-E48E8C3E-4C99-43EE-BA10-70D2B71C0B34Q51684046-CCAFF400-3B47-42DB-8816-5C54971FACB1Q54377164-5471F052-8F2F-4AEB-BD30-B4AA52CB0C6E
P2860
Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A.
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
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@en
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@nl
type
label
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@en
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@nl
prefLabel
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@en
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@nl
P2093
P2860
P356
P1433
P1476
Trifluoroethanol-induced confo ...... actalbumin and ribonuclease A.
@en
P2093
Damaschun G
Müller-Frohne M
P2860
P304
P356
10.1110/PS.8.3.625
P577
1999-03-01T00:00:00Z