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Volumn 96, Issue 1, 2011, Pages 4-13
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Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.
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Author keywords
[No Author keywords available]
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Indexed keywords
(PROLYL HYDROXYLPROLYL GLYCINE)10;
(PROLYL-HYDROXYLPROLYL-GLYCINE)10;
ARGININE;
COLLAGEN TYPE 1;
GLYCINE;
PEPTIDE;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
CHEMISTRY;
CIRCULAR DICHROISM;
DIFFERENTIAL SCANNING CALORIMETRY;
GENETICS;
HUMAN;
METABOLISM;
MOLECULAR GENETICS;
MUTATION;
OSTEOGENESIS IMPERFECTA;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
PROTEIN UNFOLDING;
THERMODYNAMICS;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARGININE;
CALORIMETRY, DIFFERENTIAL SCANNING;
CIRCULAR DICHROISM;
COLLAGEN TYPE I;
GLYCINE;
HUMANS;
MOLECULAR SEQUENCE DATA;
MUTATION;
OSTEOGENESIS IMPERFECTA;
PEPTIDES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN UNFOLDING;
THERMODYNAMICS;
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EID: 79959806152
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/bip.21432 Document Type: Article |
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Times cited : (30)
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References (0)
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