Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 17, 2011, Pages 6963-6968

  Xia, Fei ^a,b   Thirumalai, D ^c   Gräter, Frauke ^a,b  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^b HEIDELBERG INSTITUTE FOR THEORETICAL STUDIES   (Germany)

^c Bldg 142   (United States)

Author keywords

Atomic force microscopy; Folding intermediates; Self organized polymer model; Three stage refolding; Unfolding kinetics

Indexed keywords

DIMER; POLYUBIQUITIN;

ARTICLE; ATOMIC FORCE SPECTROSCOPY; CHEMICAL STRUCTURE; FORCE; MOLECULAR INTERACTION; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN FOLDING; SIMULATION; SPECTROSCOPY;

ANIMALS; HUMANS; MICROSCOPY, ATOMIC FORCE; MOLECULAR DYNAMICS SIMULATION; POLYUBIQUITIN; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 79955565416     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1018177108     Document Type: Article

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