W-F substitutions in apomyoglobin increase the local flexibility of the n-terminal region causing amyloid aggregation: A H/D exchange study

Protein and Peptide Letters

Volumn 20, Issue 8, 2013, Pages 898-904

  Infusini, Giuseppe ^a   Iannuzzi, Clara ^a   Vilasi, Silvia ^a   Maritato, Rosa ^a   Birolo, Leila ^b   Pagnozzi, Daniela ^b   Pucci, Piero ^b   Irace, Gaetano ^a   Sirangelo, Ivana ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Amyloid aggregation; Apomyoglobin; H D exchanges; Protein folding; Protein misfolding; W F substitution

Indexed keywords

AMYLOID; APOMYOGLOBIN; DEUTERIUM; HYDROGEN; PEPSIN A; PHENYLALANINE; TRYPTOPHAN; APOPROTEIN; MUTANT PROTEIN; MYOGLOBIN; PEPTIDE FRAGMENT;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; MASS SPECTROMETRY; MUTANT; NONHUMAN; PH; PHYSICAL CHEMISTRY; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; SEQUENCE ANALYSIS; SPERM WHALE; STRUCTURE ANALYSIS; WILD TYPE; CHEMISTRY; DEUTERIUM HYDROGEN EXCHANGE; METABOLISM; PROTEIN CONFORMATION;

AMYLOID; APOPROTEINS; DEUTERIUM EXCHANGE MEASUREMENT; MASS SPECTROMETRY; MUTANT PROTEINS; MYOGLOBIN; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEOLYSIS;

EID: 84880160920     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511320080006     Document Type: Article

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