Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings

Journal of Molecular Biology

Volumn 340, Issue 5, 2004, Pages 1131-1142

  Mohana Borges, Ronaldo ^a   Goto, Natalie K ^a   Kroon, Gerard J A ^a   Dyson, H Jane ^a   Wright, Peter E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

apoMb, apomyoglobin; apomyoglobin; conformational ensemble; HSQC, heteronuclear single quantum coherence; IPAP, in phase antiphase spectra; NMR; NMR, nuclear magnetic resonance; NOE, nuclear Overhauser effect; residual dipolar coupling; unfolded protein

Indexed keywords

ACID; AMIDE; APOMYOGLOBIN; BACTERIAL PROTEIN; HYDROGEN; NITROGEN; NUCLEASE; POLYACRYLAMIDE GEL; POLYMER; POLYPEPTIDE; UREA;

ARTICLE; CHEMICAL BOND; CONTROLLED STUDY; DIPOLE; LANDSCAPE; MOLECULAR BIOLOGY; MOLECULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 3242789489     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.022     Document Type: Article

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