Complete sequence-specific sup 1 H NMR assignments for human insulin

Journal Article · Tue Mar 27 04:00:00 EST 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00464a003· OSTI ID:6170423

Kline, A D; Justice, Jr, R M ^[1]

---

1. Eli Lilly and Co., Indianapolis, IN (USA)

Solvent conditions where human insulin could be studied by high-resolution NMR were determined. Both low pH and addition of acetonitrile were required to overcome the protein's self-association and to obtain useful spectra. Two hundred eighty-six {sup 1}H resonances were located and assigned to specific sites on the protein by using two-dimensional NMR methods. The presence and position of numerous d{sub NN} sequential NOE's indicate that the insulin conformation seen in crystallographic studies is largely retained under these solution conditions. Slowly exchanging protons were observed for seven backbone amide protons and were assigned to positions A15 and A16 and to positions B15-B19. These amides all occur within helical regions of the protein.

• OSTI ID: 6170423
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:12; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACIDS
ANIMALS
BARYONS
CARBOXYLIC ACIDS
CHEMICAL SHIFT
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HEAVY WATER
HORMONES
HYDROGEN COMPOUNDS
HYDROXY ACIDS
INSULIN
MAGNETIC RESONANCE
MAMMALS
MAN
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
OXYGEN COMPOUNDS
PEPTIDE HORMONES
PRIMATES
PROTONS
RESONANCE
SERINE
VERTEBRATES
WATER