Solvent and temperature effects on crambin, a hydrophobic protein

Journal Article · Wed Oct 01 00:00:00 EDT 1980 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(80)84924-1· OSTI ID:6857113

Llinas, M ^[1]; Lecomte, J T.J.; De Marco, A

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1. Carnegie-Mellon Univ., Pittsburgh, PA

Crambin, a 5000-mol. wt. water-insoluble protein found in crambe abyssinica seeds is presently being studied by x-ray diffraction to 0.9 A resolution and /sup 1/H-nuclear magnetic resonance (NMR) spectroscopy. Preliminary /sup 1/H-NMR data at 250 and 600 MHz have suggested that this hydrophobic protein retains a similar globular conformation in both glacial acetic acid (AA), a Bronsted acid, and dimethylformamide (DMF), a Lewis base. These observations suggest that the globular conformation observed in these organic solvents is most likely the native structure present in the crystalline state. As suggested by the high intrinsic resolution of the crystallographic x-ray diffraction pattern, and demonstrated by the NMR data, crambin is a very rigid protein. Work is in progress to assign the /sup 1/H-resonances and to correlate H and /sup 13/C NMR dynamic data with the crystallographic model. It is hoped that unravelling conformational features of this hydrophobic protein will provide clues to help us understand other membrane-bound functional proteins.

• OSTI ID: 6857113
• Journal Information: Biophys. J.; (United States), Vol. 32:1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
SOLVENT PROPERTIES
SPATIAL DEPENDENCE
TEMPERATURE EFFECTS
CRYSTALLOGRAPHY
MOLECULAR STRUCTURE
NMR SPECTRA
PROTEIN DENATURATION
X-RAY DIFFRACTION
COHERENT SCATTERING
DIFFRACTION
ORGANIC COMPOUNDS
SCATTERING
SPECTRA
550200* - Biochemistry