Assignment of asparagine-44 side-chain primary amide /sup 1/H NMR resonances and the peptide amide N/sup 1/H resonance of glycine-37 in basic pancreatic trypsin inhibitor
New assignments of three previously undetected amide proton NMR resonance lines in bovine pancreatic trypsin inhibitor are reported. These are the peptide amide proton of Gly-37 and the primary amide protons of Asn-44. Specific assignments of Asn-44 and Asn-43 H/sub E/ and H/sub Z/ resonances are also reported. The Gly-37 NH and Asn-44 H/sub Z/ resonances are shifted upfield to 4.3 and 3.4 ppm, respectively, by the ring current of the Tyr-35 aromatic group, while Asn-44 H/sub E/ resonates at 7.8 ppm. The abnormal chemical shifts of Asn-44 H/sub Z/ and Gly-37 NH indicate that both NH's interact with the ..pi..-electron cloud of the Tyr-35 ring. This is consistent with their location in the crystal structure. The resonances are resolved by differential labeling techniques and are studied by combined use of NOE and exchange difference spectroscopy.
- Research Organization:
- Roskilde Univ., Denmark
- OSTI ID:
- 5940773
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:7; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Assignments of sup 15 N and sup 1 H NMR resonances and a neutral pH ionization in Rhodospirillum rubrum cytochrome c sub 2
Proton resonance assignments of horse ferricytochrome c
Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
AMIDES
AMINO ACIDS
ASPARAGINE
BARYONS
CARBOXYLIC ACIDS
CHEMICAL SHIFT
ELEMENTARY PARTICLES
ENZYME INHIBITORS
ENZYMES
FERMIONS
GLYCINE
HADRONS
HYDROLASES
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDE HYDROLASES
PROTONS
RESONANCE
SERINE PROTEINASES
SPECTRA
TRYPSIN