Sequence-specific sup 1 H NMR assignments and solution structure of bovine pancreatic polypeptide

Journal Article · Tue Feb 04 00:00:00 EST 1992 · Biochemistry; (United States)

OSTI ID:5618148

Li, Xiang; Dobson, C M ^[1]; Sutcliffe, M J ^[2]; Schwartz, T W ^[3]

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1. Univ. of Oxford (United Kingdom)
2. Leicester Univ. (United Kingdom)
3. Lab. for Molecular Endocrinology, Copenhagen (Denmark)

Sequence-specific {sup 1}H NMR assignments for the 36 residue bovine pancreatic polypeptide (bPP) have been completed. The secondary and tertiary structure of bPP in solution has been determined from experimental NMR data. It is shown that bPP has a very well-defined C-terminal {alpha}-helix involving residues 15-32. Although regular secondary structure cannot be clearly defined in the N-terminal region, residues 15-32. Although regular secondary structure cannot be clearly defined in the N-terminal region, residues 4-8 maintain a rather ordered conformation in solution. This is attributed primarily to the hydrophobic interaction between this region and the C-terminal helix. The two segments of the structure are joined by a turn which is poorly defined. The four end residues both at the N-terminus and the C-terminus are highly disordered in solution. The overall fold of the bPP molecule is very closely similar to that found in the crystal structure of avian pancreatic polypeptide (aPP). The RMS deviation for backbone atoms of residues 4-8 and 15-32 between the bPP mean structure and the aPP crystal structure is 0.65 {angstrom}, although there is only 39% identity of the residues. Furthermore, the average conformations of some (mostly from the {alpha}-helix) side chains of bPP in solution are closely similar to those of aPP in the crystal structure. A large number of side chains of bPP, however, show significant conformational averaging in solution.

• OSTI ID: 5618148
• Journal Information: Biochemistry; (United States), Vol. 31:4; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
POLYPEPTIDES
NUCLEAR MAGNETIC RESONANCE
CATTLE
CHEMICAL SHIFT
OVERHAUSER EFFECT
PANCREAS
PROTONS
ANIMALS
BARYONS
BODY
DIGESTIVE SYSTEM
DOMESTIC ANIMALS
ELEMENTARY PARTICLES
ENDOCRINE GLANDS
FERMIONS
GLANDS
HADRONS
MAGNETIC RESONANCE
MAMMALS
NUCLEONS
ORGANIC COMPOUNDS
ORGANS
PEPTIDES
PROTEINS
RESONANCE
RUMINANTS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques