Normal mode analysis of mouse epidermal growth factor: Characterization of the harmonic motion
- 1 August 1993
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 16 (4) , 423-436
- https://doi.org/10.1002/prot.340160410
Abstract
Normal mode analysis of mouse epidermal growth factor (mEGF) has been carried out at room temperature. The value of the lowest frequency is 4.1 cm−1. This mode corresponds to hinge-bending motion between the N-terminal and C-terminal domains of mEGF. This hinge-bending motion corresponds to the “mitten mode.” In this motion, the N-terminal domain is almost rigid. However, the C-terminal domain is found to consist of three rigid segments. Two segments, C33-D46 and G51-R53, are observed moving in the same direction, but L47-W50 moves in the opposite direction. For this mode, the effective Young's modulus turned out to be 1.1 × 109 dyn·−2. This value is a little larger than that of the mode with the lowest frequency 4.4 cm−1 of BPTI. The difference may be related to the fraction of residues involved in β-sheets in the molecule. Similar analyses are carried out for other low frequency modes.Keywords
This publication has 14 references indexed in Scilit:
- Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraintsBiochemistry, 1992
- Biochemical properties of site-directed mutants of human epidermal growth factor: the importance of solvent-exposed hydrophobic residues of the amino-terminal domain in receptor bindingBiochemistry, 1990
- Normal mode analysis of human lysozyme: Study of the relative motion of the two domains and characterization of the harmonic motionProteins-Structure Function and Bioinformatics, 1990
- Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.Proceedings of the National Academy of Sciences, 1987
- Normal modes of vibration in bovine pancreatic trypsin inhibitor and its mechanical propertyProteins-Structure Function and Bioinformatics, 1987
- Calculation of protein conformations by proton-proton distance constraintsJournal of Molecular Biology, 1985
- Sustained release of epidermal growth factor accelerates wound repair.Proceedings of the National Academy of Sciences, 1985
- Autocrine growth factors and cancerNature, 1985
- Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1983
- Autocrine Secretion and Malignant Transformation of CellsNew England Journal of Medicine, 1980