= M. Bycroft
{c}
M. Bycroft is the first-named author of a 1997 structural study of the <S1 RNA-binding domain>. The paper examined this <protein domain> from <Escherichia coli> <polynucleotide phosphorylase> using <nuclear magnetic resonance>. Its initial-only byline is retained here.<The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold by M. Bycroft and others>[Published byline and abstract]{ref}
The resulting <protein structure> contained a five-stranded antiparallel <beta barrel>. Conserved <amino acid residues> and neighboring loops suggested a possible <RNA>-binding face. Comparing this fold with other <proteins> connected a small structural module with a broader family of nucleic-acid interactions.<The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold by M. Bycroft and others>[Abstract: solution structure, putative RNA-binding face and related proteins]{ref}
The distinction between an observed fold and a proposed binding face is scientifically useful. Finding several conserved <amino acid residues> on the same exposed surface suggests an experiment: alter selected residues, then compare <RNA> binding while independently checking whether the <protein> still folds. Weaker binding after a change that also unfolds the <protein> would not establish a direct contact at that residue. This is an experimental interpretation of the structural hypothesis, not a report that every such test was performed in the 1997 paper.
For a simple architectural example, two <proteins> can each contain one <S1 RNA-binding domain> while having different additional <protein domains>. Sharing that module alone does not imply identical <enzyme> activity, the same <RNA> preference, or an equal number of <active sites>.
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