Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids

Proceedings of the National Academy of Sciences of the United States of America

Volumn 92, Issue 20, 1995, Pages 9014-9018

  Dietrich, Christian ^a   Schmitt, Lutz ^a   Tampé, Robert ^a,b  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

film balance; fluorescence microscopy; membranes; protein engineering; supramolecular assemblies

Indexed keywords

CHELATE; GENE PRODUCT; HISTIDINE; HYBRID PROTEIN; LIPID; METAL ION; NITRILOTRIACETIC ACID;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CHELATION; CRYSTALLIZATION; FLUORESCENCE MICROSCOPY; INFRARED SPECTROSCOPY; MOLECULAR BIOLOGY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; THIN LAYER CHROMATOGRAPHY;

AMINES; AMINO ACID SEQUENCE; CHELATING AGENTS; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HISTIDINE; INDICATORS AND REAGENTS; MODELS, STRUCTURAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; NITRILOTRIACETIC ACID; PEPTIDES; PHOSPHATIDYLETHANOLAMINES; RECOMBINANT FUSION PROTEINS; SEQUENCE TAGGED SITES; SUPPORT, NON-U.S. GOV'T;

EID: 0029025914     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.20.9014     Document Type: Article

References (14)