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Article

The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.

Journal of molecular biology - 6 Jun 2003

Millet Oscar, Mittermaier Anthony, Baker David, Kay Lewis E

Abstract excerpt

Recently developed 2H spin relaxation experiments are applied to study the dynamics of methyl-containing side-chains in the B1 domain of protein L and in a pair of point mutants of the domain, F22L and A20V. X-ray and NMR studies of the three variants of protein L studied here establish that their structures are very similar, despite the fact that the F22L mutant is 3.2kcal/mol less stable. Measurements of methyl...

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Identifiers

PMID: 12767834
DOI: 10.1016/s0022-2836(03)00471-6

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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