![]() |
Volumn 25, Issue 11, 2012, Pages 699-703
|
A highly stable protein chimera built from fragments of different folds
|
Author keywords
( )8 barrel; chimera; flavodoxin like; hybrid proteins; protein design
|
Indexed keywords
CHEMICAL DENATURATION;
CHIMERA;
CHIMERIC PROTEINS;
DESIGN STRATEGIES;
FLAVODOXIN-LIKE;
NOVEL FOLDS;
PROTEIN DESIGN;
PROTEIN FOLDS;
CHEMICAL STABILITY;
CURRICULA;
PROTEIN FOLDING;
PROTEINS;
PROTEIN;
CHIMERA;
CONFERENCE PAPER;
ESCHERICHIA COLI;
GENE;
MOLECULAR EVOLUTION;
MOLECULAR WEIGHT;
NONHUMAN;
OLIGOMERIZATION;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN ANALYSIS;
PROTEIN DENATURATION;
PROTEIN ENGINEERING;
PROTEIN EXPRESSION;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
BACTERIAL PROTEINS;
CLONING, MOLECULAR;
DNA-BINDING PROTEINS;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HOT TEMPERATURE;
MODELS, MOLECULAR;
PROPIONIBACTERIUM;
PROTEIN DENATURATION;
PROTEIN ENGINEERING;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE, SECONDARY;
RECOMBINANT FUSION PROTEINS;
THERMOTOGA MARITIMA;
|
EID: 84868531723
PISSN: 17410126
EISSN: 17410134
Source Type: Journal
DOI: 10.1093/protein/gzs074 Document Type: Conference Paper |
Times cited : (22)
|
References (20)
|