Synporins--synthetic proteins that emulate the pore structure of biological ionic channels.
about
Structural and biophysical properties of a synthetic channel-forming peptide: designing a clinically relevant anion selective pore.How did cells get their size?Structure and dynamics of polypeptides and proteins in lipid membranes.Total chemical synthesis, characterization, and immunological properties of an MHC class I model using the TASP concept for protein de novo design.Design of a functional calcium channel protein: inferences about an ion channel-forming motif derived from the primary structure of voltage-gated calcium channelsTemplate-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein.Synthetic Peptide templates for molecular recognition: recent advances and applications.Structural and functional studies of a synthetic peptide mimicking a proposed membrane inserting region of a Bacillus thuringiensis delta-endotoxin.Channel formation by antiapoptotic protein Bcl-2.Synthetic, biologically active amphiphilic peptidesEffect of diaminopropionic acid (Dap) on the biophysical properties of a modified synthetic channel-forming peptide.A molecular blueprint for the pore-forming structure of voltage-gated calcium channels.Modulation of the conductance of a 2,2'-bipyridine-functionalized peptidic ion channel by Ni2+.Peptide models for membrane channels.The C- and N-Terminal Residues of Synthetic Heptapeptide Ion Channels Influence Transport Efficacy Through Phospholipid Bilayers.Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A.Chemical synthesis and single channel properties of tetrameric and pentameric TASPs (template-assembled synthetic proteins) derived from the transmembrane domain of HIV virus protein u (Vpu).Identification of an ion channel-forming motif in the primary structure of tetanus and botulinum neurotoxins.Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor.Crystallographic Realization of the Mathematically Predicted Densest All-Pentagon Packing Lattice by C5-Symmetric “Sticky” FluoropentamersA pair of pyrene groups as a conformational probe for designed two α-helix polypeptidesA pair of pyrene groups as a conformational probe for designed four-α-helix bundle polypeptides
P2860
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P2860
Synporins--synthetic proteins that emulate the pore structure of biological ionic channels.
description
1990 nî lūn-bûn
@nan
1990 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Synporins--synthetic proteins ...... of biological ionic channels.
@ast
Synporins--synthetic proteins ...... of biological ionic channels.
@en
type
label
Synporins--synthetic proteins ...... of biological ionic channels.
@ast
Synporins--synthetic proteins ...... of biological ionic channels.
@en
prefLabel
Synporins--synthetic proteins ...... of biological ionic channels.
@ast
Synporins--synthetic proteins ...... of biological ionic channels.
@en
P2093
P2860
P356
P1476
Synporins--synthetic proteins ...... of biological ionic channels.
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.18.6929
P407
P577
1990-09-01T00:00:00Z