= J. Bella
{c}
<J. Bella> is the first author of a 1994 <X-ray crystallography> study of a <collagen>-like <peptide>. The structure, determined at 1.9 angstrom resolution, resolved a <collagen triple helix> and the surrounding <water> network. It connected the overall three-chain organization with individual <hydrogen bonds> and interactions involving <hydroxyproline> residues.<Crystal and molecular structure of a collagen-like peptide at 1.9 angstrom resolution by J. Bella and others>[Abstract; Science 266, 75–81, 1994]{ref}
The <peptide> contained a single <glycine>-to-<alanine> substitution. Near that position, the three-chain structure untwisted locally and water-mediated connections replaced some direct interchain <hydrogen bonds>. This gives a concrete example of how one change in <protein primary structure> can alter a local structural arrangement without erasing the whole fold. The observation concerns the studied <peptide> crystal; proposed parallels with mutant <collagen> in tissues are a further biological interpretation.<Crystal and molecular structure of a collagen-like peptide at 1.9 angstrom resolution by J. Bella and others>[Abstract: substitution site, local untwisting and water bridges]{ref}
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