Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy
about
Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylationBinding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability.Thermal stability and aggregation of sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications.Cholesterol effects on nicotinic acetylcholine receptor.Adoption of beta structure by the inactivating "ball" peptide of the Shaker B potassium channel.A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core.Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the proteinStability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse.N-type inactivation of the potassium channel KcsA by the Shaker B "ball" peptide: mapping the inactivating peptide-binding epitope.Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH.Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein.Structural properties of the putative fusion peptide of hepatitis B virus upon interaction with phospholipids. Circular dichroism and Fourier-transform infrared spectroscopy studies.Structural stabilization of botulinum neurotoxins by tyrosine phosphorylation.Structural investigation of transglutaminase by Fourier transform infrared spectroscopy.
P2860
Q28910375-39BEB561-7551-49B0-A6E9-6173CADC9C82Q30344056-7DB1B999-23D0-40B0-A001-44885266EC10Q33195739-EF9826A0-4508-4645-B0BE-70A72759F472Q36994555-74E48A97-F2CE-42EF-A524-34E7B9C3A351Q39653551-F505C9BD-81B2-420D-BDB1-B518E35ABD0CQ39787948-106ACB21-3FE7-4B05-B0B5-07F7BB151DF7Q42013387-942134DE-EA0B-4B1C-8B25-98419AB50BA5Q42164198-CE659003-9C80-4A90-BE69-7C27B42F51DAQ42652978-A1F70EDF-B5D9-4230-AB2B-51B310B58BC0Q42995901-D639048C-898F-409A-B298-C6F5A955D468Q44444501-58FE9ACE-1CAF-4633-AFE3-71ABFE5DFBDDQ44756395-D5527F62-F795-4588-8F5C-9751D6AC6D46Q45765634-334CB213-96EF-4D46-B758-CF283345EDA8Q47871406-4D30C25A-D87F-4720-BD90-43C53B436709Q53851251-EC2C8F8E-F0A0-49BD-A4BE-2A625C1E7E7B
P2860
Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy
description
1992 nî lūn-bûn
@nan
1992 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Protein stability and interact ...... ransform infrared spectroscopy
@ast
Protein stability and interact ...... ransform infrared spectroscopy
@en
type
label
Protein stability and interact ...... ransform infrared spectroscopy
@ast
Protein stability and interact ...... ransform infrared spectroscopy
@en
prefLabel
Protein stability and interact ...... ransform infrared spectroscopy
@ast
Protein stability and interact ...... ransform infrared spectroscopy
@en
P2093
P2860
P356
P1433
P1476
Protein stability and interact ...... ransform infrared spectroscopy
@en
P2093
Arrondo JL
Castresana J
Fernandez-Ballester G
Ferragut JA
Gonzalez-Ros JM
P2860
P304
P356
10.1042/BJ2880421
P407
P478
288 ( Pt 2)
P577
1992-12-01T00:00:00Z