Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding.
about
Conformational and thermodynamic properties of peptide binding to the human S100P proteinEffective energy function for proteins in solutionUnfolding studies of the cysteine protease baupain, a papain-like enzyme from leaves of Bauhinia forficata: effect of pH, guanidine hydrochloride and temperature.NMR chemical shift analysis of the conformational transition between the monomer and tetramer of melittin in an aqueous solution.Theory and application of fluorescence homotransfer to melittin oligomerizationHydrophobic hydration of amphipathic peptidesUltraviolet Raman examination of the environmental dependence of bombolitin I and bombolitin III secondary structureCytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptideSensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.Conformational sampling of peptides in cellular environments.Identification of inhibitors of melittin using nonsupport-bound combinatorial libraries.Incorporation of 2,3-diaminopropionic acid into linear cationic amphipathic peptides produces pH-sensitive vectors.Melittin-lipid bilayer interactions and the role of cholesterol.Structure and dynamics of melittin in lysomyristoyl phosphatidylcholine micelles determined by nuclear magnetic resonance.Antibacterial properties of dermaseptin S4 derivatives under extreme incubation conditions.Thermal unfolding of tetrameric melittin: comparison with the molten globule state of cytochrome cCharacterization of a new four-chain coiled-coil: influence of chain length on stability.NMR studies on the monomer-tetramer transition of melittin in an aqueous solution at high and low temperatures.The role of amphipathicity in the folding, self-association and biological activity of multiple subunit small proteins.Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides.A New Mixed All-Atom/Coarse-Grained Model: Application to Melittin Aggregation in Aqueous Solution.Evaluation of the calmodulin-SOX9 interaction by "magnetic fishing" coupled to mass spectrometry.
P2860
Q24644962-F2D3A19C-7A1F-48BE-9D90-E9FD19C58FF3Q28142746-AE443BE3-F37D-426E-82BA-CADC09814C97Q30357220-4DE7C624-950A-4313-8413-E4A514AA40D4Q31031700-25E7DAD9-34D8-4338-9579-7FE53193A23BQ34047406-67310C46-42EB-4809-80FC-9C7DD135D410Q34170112-21A5664C-0E7D-435B-88EB-E53AF7CAA7BAQ34170692-0DC00637-B702-4E47-9F58-BDD1B90D6E3DQ35585206-485AA6D6-8835-4260-A8A4-6268D8EBA973Q35705907-57CA3FA0-E5D7-4BA4-A899-3C363BE4A0C9Q36344939-A9F8F253-D534-4DEF-83C5-530239BC79D8Q36798556-A8B76DC4-B0DF-4C5B-9C59-BCAC3ACA1283Q39702833-F167DA63-D873-477C-9F73-4C4F7831C2F8Q41867473-2A4C128D-B5F1-464B-B732-73828C7EA0D1Q42067285-E1671D0F-BA5F-4583-9963-A49017BB510DQ42218485-A72F9D84-2C5A-49AA-AB06-0B9AE51B75BEQ42844397-A6532975-08E9-4293-B9F1-D53FCF67A184Q42844838-F4321EF5-C0BB-42B2-8F53-E65C9E6D3B5EQ44016629-C1DF3EBD-2EC2-4453-AE8A-10AF5ED1D504Q46826967-ED156F0B-8CA2-430C-A11F-38A73DD340C5Q47432953-929A37DE-B597-402E-9836-0DC916184F7CQ47997409-5ABAF1C1-C19B-4371-8D51-EE9A30EB97D4Q52653761-B7BF9170-A831-4C14-AF82-B76CF6687206
P2860
Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding.
description
1992 nî lūn-bûn
@nan
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
1992年论文
@zh
1992年论文
@zh-cn
name
Thermodynamics of melittin tet ...... lications for protein folding.
@en
type
label
Thermodynamics of melittin tet ...... lications for protein folding.
@en
prefLabel
Thermodynamics of melittin tet ...... lications for protein folding.
@en
P2860
P356
P1433
P1476
Thermodynamics of melittin tet ...... lications for protein folding.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560010510
P577
1992-05-01T00:00:00Z