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Volumn 528, Issue 2, 2012, Pages 118-126
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An Arg-rich putative prebiotic protein is as stable as its Lys-rich variant
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Author keywords
Circular dichroism; Conformational stability; Nuclear magnetic resonance; Prebiotic Earth; RNA protein interactions
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Indexed keywords
ALANINE;
ARGININE;
GLYCINE;
ISOLEUCINE;
KIA7 PEPTIDE;
LYSINE;
PEPTIDE;
PREBIOTIC AGENT;
RIA7 PEPTIDE;
RNA;
TYROSINE;
UNCLASSIFIED DRUG;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CIRCULAR DICHROISM;
DEUTERIUM HYDROGEN EXCHANGE;
ELECTROPHORESIS;
FLUORESCENCE SPECTROSCOPY;
HYDROPHOBICITY;
LIGAND BINDING;
LIGHT SCATTERING;
NUCLEAR MAGNETIC RESONANCE;
PRIORITY JOURNAL;
PROTEIN DENATURATION;
PROTEIN ENGINEERING;
PROTEIN FOLDING;
PROTEIN STRUCTURE;
AMINO ACID SEQUENCE;
ARGININE;
BASE SEQUENCE;
BIOGENESIS;
CIRCULAR DICHROISM;
DEUTERIUM EXCHANGE MEASUREMENT;
EARTH (PLANET);
LYSINE;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
NUCLEIC ACID CONFORMATION;
PEPTIDES;
PROTEIN FOLDING;
PROTEIN MULTIMERIZATION;
PROTEIN STABILITY;
PROTEIN STRUCTURE, SECONDARY;
RNA;
SPECTROMETRY, FLUORESCENCE;
THERMODYNAMICS;
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EID: 84867641733
PISSN: 00039861
EISSN: 10960384
Source Type: Journal
DOI: 10.1016/j.abb.2012.09.006 Document Type: Article |
Times cited : (5)
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References (65)
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