Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins

Biophysical Journal

Volumn 104, Issue 8, 2013, Pages 1740-1751

  Silvestre Ryan, Jordi ^a   Bertoncini, Carlos W ^a   Fenwick, Robert Bryn ^a   Esteban Martin, Santiago ^b   Salvatella, Xavier ^a,c  

^a INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^b BARCELONA SUPERCOMPUTING CENTER   (Spain)

^c INSTITUCIÓ CATALANA DE RECERCA I ESTUDIS AVANÇATS ICREA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; APOPROTEIN; MYOGLOBIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; HUMAN; MOLECULAR DYNAMICS; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING;

AMINO ACID SEQUENCE; APOPROTEINS; HUMANS; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; MYOGLOBIN; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 84876351687     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.02.019     Document Type: Article

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