The two tryptophans of 2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure

BMC Evolutionary Biology

Volumn 11, Issue 1, 2011, Pages

  Raimondi, Sara ^a   Barbarini, Nicola ^a   Mangione, Palma ^a   Esposito, Gennaro ^b   Ricagno, Stefano ^c   Bolognesi, Martino ^c   Zorzoli, Irene ^a   Marchese, Loredana ^a   Soria, Cristina ^a   Bellazzi, Riccardo ^a   Monti, Maria ^d   Stoppini, Monica ^a,b   Stefanelli, Mario ^a   Magni, Paolo ^a   Bellotti, Vittorio ^a  

^a UNIVERSITY OF PAVIA   (Italy)

^b UNIVERSITY OF UDINE   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

^d UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLOGRAPHY; ENZYME; EVOLUTIONARY BIOLOGY; HYDROPHOBICITY; IMMUNITY; PHYLOGENETICS; PROTEIN; THERMODYNAMICS;

AMYLOID; BETA 2 MICROGLOBULIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; BETA 2-MICROGLOBULIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; TRYPTOPHAN;

EID: 79958178306     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-11-159     Document Type: Article

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