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NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B)[SIGNALING PROTEIN]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A)[SIGNALING PROTEIN]
NMR-driven structure of KRAS4B-GDP homodimer on a lipid bilayer nanodisc[ONCOPROTEIN]
NMR-driven structure of KRAS4B-GTP homodimer on a lipid bilayer nanodisc[ONCOPROTEIN]
MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs[LIPID BINDING PROTEIN]
MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs[LIPID BINDING PROTEIN]
The 3D solution structure of discoidal high-density lipoprotein particles[LIPID BINDING PROTEIN]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc[LIPID BINDING PROTEIN]
View in iCn3D PubMedProteinsConserved DomainsPubChem Compound
NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc[LIPID BINDING PROTEIN]
NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc[LIPID BINDING PROTEIN]
2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization[LIPID TRANSPORT]
Solution structure of double super helix model[LIPID BINDING PROTEIN]
PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:DPC MOLE RATIO OF 1:40[LIPID TRANSPORT]
View in iCn3D PubMedProteins
PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40[LIPID TRANSPORT]
PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.6, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40[LIPID TRANSPORT]
THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE[HIGH DENSITY LIPOPROTEINS]
CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I[LIPID TRANSPORT]
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