Ca2+-loaded spherulin 3a from physarum polycephalum adopts the prototype γ-crystallin fold in aqueous solution

Journal of Molecular Biology

Volumn 271, Issue 4, 1997, Pages 645-655

  Rosinke, Burkhard ^a   Renner, Christian ^a   Mayr, Eva Maria ^b   Jaenicke, Rainer ^b   Holak, Tad A ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

NMR; Physarum polycephalum; Protein evolution; Spherulin structure; crystallin superfamily

Indexed keywords

CALCIUM ION; CARBON 13; CELL PROTEIN; GAMMA CRYSTALLIN; LENS PROTEIN; NITROGEN 15; PROTEIN PRECURSOR; RECOMBINANT PROTEIN; SPHERULIN; UNCLASSIFIED DRUG; CALCIUM; COCCIDIOIDIN; CRYSTALLIN; FUNGAL PROTEIN; PROTOZOAL PROTEIN; SPHERULIN 3A PROTEIN, PHYSARUM POLYCEPHALUM;

AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ISOTOPE LABELING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; OLIGOMERIZATION; PHYSARUM POLYCEPHALUM; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; HYDROGEN BOND; MOLECULAR GENETICS; ULTRASTRUCTURE;

BOVINAE; CHONDROMYCES; ESCHERICHIA; MYXOGASTRIA; PHYSARUM POLYCEPHALUM; STAPHYLOCOCCUS PHAGE 3A; VERTEBRATA;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM; COCCIDIOIDIN; CRYSTALLINS; FUNGAL PROTEINS; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PHYSARUM POLYCEPHALUM; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTOZOAN PROTEINS; RECOMBINANT PROTEINS;

EID: 0030610919     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1184     Document Type: Article

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