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Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins
Author(s) -
Tugarinov Vitali,
Kay Lewis E.
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500110
Subject(s) - biomolecule , protonation , chemistry , monomer , molecule , residue (chemistry) , molecular dynamics , small molecule , computational chemistry , biochemistry , organic chemistry , polymer , ion
Solution NMR studies of biomolecules are typically limited by the molecules' molecular weight. Here we report strategies based on the use of highly deuterated, methyl‐protonated proteins that facilitate both structural and motional studies of molecules on the order of 100 kDa. Approaches and concepts are illustrated with applications to the enzyme malate synthase G, a monomeric 723‐residue protein.