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Volumn 508, Issue 3, 2001, Pages 427-432
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Two parameters improve efficiency of mitochondrial uptake of adenylate kinase: Decreased folding velocity and increased propensity of N-terminal α-helix formation
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Author keywords
Adenylate kinase; Mitochondrial import; Protein folding; Saccharomyces cerevisiae; Sub mitochondrial sorting
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Indexed keywords
ADENYLATE KINASE;
ALPHA HELIX;
AMINO ACID SEQUENCE;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING AFFINITY;
CELLULAR DISTRIBUTION;
CONTROLLED STUDY;
CYTOPLASM;
DENATURATION;
KINETICS;
MITOCHONDRION;
MUTANT;
MUTATION;
NONHUMAN;
PARAMETER;
PRIORITY JOURNAL;
PROBABILITY;
PROTEIN FOLDING;
PROTEIN INTERACTION;
PROTEIN MODIFICATION;
PROTEIN STRUCTURE;
RENATURATION;
STEADY STATE;
YEAST;
ADENYLATE KINASE;
ENZYME PRECURSORS;
ENZYME STABILITY;
INTRACELLULAR MEMBRANES;
MEMBRANE POTENTIALS;
MITOCHONDRIA;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN RENATURATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN TRANSPORT;
VALINOMYCIN;
YEASTS;
EUKARYOTA;
SACCHAROMYCES CEREVISIAE;
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EID: 0035941127
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(01)03122-2 Document Type: Article |
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Times cited : (8)
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References (43)
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