Chris Oubridge
= Chris Oubridge
{c}
{tag=Biology author}
{title2=1966-2020}
= C. Oubridge
{c}
{synonym}
\b[Chris Oubridge] investigated the structural basis of <RNA splicing> and <RNA> recognition by <proteins>. The original 1994 publisher record names him as first author of the <U1A protein>–<RNA hairpin> structure previously cited under C. Oubridge.<Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin by C. Oubridge and others>[Publisher byline and Abstract, DOI10.1038/372432a0]{ref} His institutional obituary records 1966–2020 and describes his contributions to <spliceosome> structural studies.<Chris Oubridge obituary at the MRC Laboratory of Molecular Biology>[Named heading and research account]{ref}
The 1994 <X-ray crystallography> study resolved an RNA-binding domain with a 21-<nucleotide> <RNA hairpin> with a resolution of 1.92 angstroms. Its ten-<nucleotide> loop lies on the domain's <beta sheet>; contacts involving the loop sequence include <hydrogen bonds>. This provides a physical explanation of sequence recognition, rather than treating a matching letter sequence as sufficient without a compatible <RNA> structure.<Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin by C. Oubridge and others>[Abstract, loop conformation and protein–RNA contacts]{ref}
For an original affinity example, suppose changing a loop raises a measured <dissociation constant> from $10$ to $100\,\mathrm{nM}$. At 298 <kelvin>, the corresponding change in standard binding <Gibbs free energy> is
$$
\Delta\Delta G^\circ=RT\ln\frac{K_{d,2}}{K_{d,1}}
=RT\ln10\approx5.7\ \mathrm{kJ\,mol^{-1}},
$$
where $R$ is the <molar gas constant>. These are stipulated values, not measurements from the 1994 paper. A structure can motivate which contacts to test, while an independent <binding affinity> measurement establishes the net energetic effect; counting visible contacts alone does not supply that effect.
Oubridge also shared first authorship of the 2009 <U1 snRNP> functional-core structure, connecting the study of an individual recognition domain with the arrangement of <RNA> and <proteins> in a larger assembly.<Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution by Daniel A. Pomeranz Krummel and others>[Byline, equal-contribution note and Abstract]{ref}
\Image[https://mrclmb.ac.uk/wp-content/uploads/archive-news-Oubridge_J126751_Obit.jpg]
{title=Chris Oubridge in the laboratory, named photograph in the MRC Laboratory of Molecular Biology obituary}
{height=300}