Shift of fibril-forming ability of the designed α-helical coiled-coil peptides into the physiological pH region

Protein Engineering

Volumn 16, Issue 12, 2003, Pages 1125-1130

  Melnik, T N ^a   Villard, V ^b   Vasiliev, V ^a   Corradin, G ^b   Kajava, A V ^c   Potekhin, S A ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b UNIVERSITY OF LAUSANNE   (Switzerland)

^c Centre National de la Recherche Scientifique   (France)

Author keywords

Design; Fibrils; Peptides; Physico chemical characteristics

Indexed keywords

ALPHA HELICAL FIBRIL FORMING PEPTIDE; GLUTAMIC ACID; GLUTAMINE; PEPTIDE; SERINE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; BIOMEDICINE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; DIFFUSION; ELECTRICITY; ELECTRON MICROSCOPY; FIBER; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SEDIMENTATION;

CALORIMETRY; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ELECTRON; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 1442359484     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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