Article
NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Biochemistry - 10 Apr 1990
Redfield A G, Papastavros M Z
Abstract excerpt
The structure of the phosphoryl binding region of human N-ras p21 was probed by using heteronuclear proton-observed NMR methods. Normal protein and a Gly-12----Asp-12 mutant protein were prepared with two amino acids labeled with 15N at their amide positions: valine and glycine, aspartic acid and glycine, and lysine and glycine. We completed the identification of amide 15NH resonances from Gly-12 and Asp-12 to...
Topics
- Amino Acid Sequence
- Aspartic Acid
- Binding Sites
- Escherichia coli
- Glycine
- Guanosine Diphosphate
- Hydrogen Bonding
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Oncogene Protein p21(ras)