![PDF) Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the proα1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability PDF) Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the proα1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability](https://i1.rgstatic.net/publication/15711037_Substitutions_of_aspartic_acid_for_glycine-220_and_of_arginine_for_glycine-664_in_the_triple_helix_of_the_proa1I_chain_of_type_I_procollagen_produce_lethal_osteogenesis_imperfecta_and_disrupt_the_abil/links/542032680cf203f155c2b23c/largepreview.png)
PDF) Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the proα1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability
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SOLVED:ABBREVIATION 3-Letter 1-Letter ABBREVIATION 3-Letter 1-Letter Amino Acid Amino Acid Alanine Ala Arginine Arg Asparagine Asn Aspartic acid Asp Cysteine Cys Glutamic acid Glu Glutamine GIn Glycine Gly Histidine His Isoleucine Ile
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Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step | Communications Biology
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