Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein

Protein Science

Volumn 8, Issue 8, 1999, Pages 1675-1688

  Padmanabhan, S ^a   Jiménez, M Angeles ^a   Rico, Manuel ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

Author keywords

434 Cro; Helices; Peptide conformation; Peptide NMR; Protein folding

Indexed keywords

REPRESSOR PROTEIN; UREA; WATER;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE; CIRCULAR DICHROISM; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING;

BACTERIOPHAGE 434; BACTERIOPHAGE LAMBDA;

EID: 0345362966     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.8.1675     Document Type: Article

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