Formation of supramolecular structures of a native-like protein in the presence of amphiphilic peptides: Variations in aggregate morphology

FEBS Letters

Volumn 586, Issue 2, 2012, Pages 186-190

  Artemova, Natalya ^a   Stein Margolina, Vita ^a   Smirnova, Ekaterina ^a   Gurvits, Bella ^a  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

Author keywords

Amphiphilic peptide; Dynamic light scattering; Electron microscopy; Protein aggregation; Supramolecular structure

Indexed keywords

ALCOHOL DEHYDROGENASE; AMPHOPHILE; AMYLOID; ARGINYLPHENYLALANINE; ASPARTYLPHENYLALANINE; DIPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DYNAMIC LIGHT SCATTERING; ENZYME KINETICS; FLUORESCENCE SPECTROSCOPY; HEAT TREATMENT; HYDROPHOBICITY; LIGHT SCATTERING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SUPRAMOLECULAR CHEMISTRY; SUPRAMOLECULAR STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; YEAST;

ALCOHOL DEHYDROGENASE; ANIMALS; CATTLE; CHEMICAL PRECIPITATION; LACTALBUMIN; MICROSCOPY, ATOMIC FORCE; MULTIPROTEIN COMPLEXES; MURAMIDASE; PEPTIDES; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE-ACTIVE AGENTS; TIME FACTORS; YEASTS;

EID: 84855821706     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.12.017     Document Type: Article

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