Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface.
about
Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.Interaction of dystrophin rod domain with membrane phospholipids. Evidence of a close proximity between tryptophan residues and lipids.Activation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.Structural dynamics of a lytic peptide interacting with a supported lipid bilayerRapid segmental and subdomain motions of DNA polymerase beta.
P2860
Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface.
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
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@wuu
2000年论文
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2000年论文
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name
Site-specific tryptophan dynam ...... hospholipid bilayer interface.
@en
type
label
Site-specific tryptophan dynam ...... hospholipid bilayer interface.
@en
prefLabel
Site-specific tryptophan dynam ...... hospholipid bilayer interface.
@en
P2860
P1433
P1476
Site-specific tryptophan dynam ...... hospholipid bilayer interface.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(00)76360-0
P407
P577
2000-08-01T00:00:00Z