Solution structure of apamin determined by nuclear magnetic resonance and distance geometry

Journal Article · Tue Nov 01 00:00:00 EST 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00422a029· OSTI ID:6206374

Pease, J H.B.; Wemmer, D E

The solution structure of the bee venom neurotoxin apamin has been determined with a distance geometry program using distance constraints derived from NMR. Twenty embedded structures were generated and refined by using the program DSPACE. After error minimization using both conjugate gradient and dynamics algorithms, six structures had very low residual error. Comparisons of these show that the backbone of the peptide is quite well-defined with the largest rms difference between backbone atoms in these structures of 1.34 /Angstrom/. The side chains have far fewer constraints and show greater variability in their positions. The structure derived here is generally consistent with the qualitative model previously described, with most differences occurring in the loop between the ..beta..-turn (residues 2-5) and the C-terminal ..cap alpha..-helix (residues 9-17). Comparisons are made with previously derived models from NMR data and other methods.

• Research Organization: Lawrence Berkeley Lab., CA (USA)
• DOE Contract Number: AC03-76SF00098
• OSTI ID: 6206374
• Journal Information: Biochemistry; (United States), Vol. 27:22
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
TOXINS
MOLECULAR STRUCTURE
AQUEOUS SOLUTIONS
CHEMICAL SHIFT
HEAVY WATER
NUCLEAR MAGNETIC RESONANCE
PROTONS
STEREOCHEMISTRY
ANTIGENS
BARYONS
DISPERSIONS
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
MAGNETIC RESONANCE
MATERIALS
MIXTURES
NUCLEONS
OXYGEN COMPOUNDS
RESONANCE
SOLUTIONS
TOXIC MATERIALS
WATER
550601* - Medicine- Unsealed Radionuclides in Diagnostics