title: NMR assignments of the binary hvDHFR1:folate complex.
abstract: A better understanding of how salt affects enzyme activity can be gained via NMR studies of binary hvDHFR1:folate complex. Chemical shift assignments of the 17.9 kDa enzyme with bound substrate prepare the way for ongoing research of the effects of salt on enzyme flexibility through relaxation studies.
authors.affiliation: Department of Chemistry, Mississippi State University, Box 9573, Mississippi State, MS 39762, USA.
authors.forename: Arezue F B
authors.initials: AF
authors.lastname: Boroujerdi
authors.forename: Bulent
authors.initials: B
authors.lastname: Binbuga
authors.forename: John K
authors.initials: JK
authors.lastname: Young
mesh_terms: D005492:Folic Acid / Q000737:chemistry; D019622:Haloferax volcanii / Q000201:enzymology* / Q000235:genetics; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D054712:Salinity; D013379:Substrate Specificity; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D005492:Folic Acid; D013762:Tetrahydrofolate Dehydrogenase