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Can I read Folding and Function of the Myelin Proteins from Primary Sequence Data on EtoBox?
Folding and Function of the Myelin Proteins from Primary Sequence Data by Dr. H. Inouye; Dr. D. A. Kirschner is a Neuroscience article available to read on EtoBox.
What is Folding and Function of the Myelin Proteins from Primary Sequence Data about?
To explain how the myelin proteins are involved in the organization and function of the myelin sheath requires knowing their molecular structures. Except for P2 basic protein of PNS myelin, however, their structures are not yet known. As an aid to predicting their molecular folding and possible functions, we have developed a FORTRAN program to analyze the primary sequence data for proteins, and have applied this to the myelin proteins in particular. In this program, propensities for the secondary structure conformations as well as physical-chemical parameters are assigned to the amino acids and the pattern of these parameters is examined by calculating their average values, autocorrelation functions and Fourier transforms. To compare two proteins, their sequences are aligned using a unitary scoring matrix, and homologies are searched by plotting a two-dimensional map of the correlation coefficients. Comparison of the corresponding myelin basic proteins (MBP) and PO glycoproteins (PO) for rodent and shark showed that the conserved residues included most of the amino acids which were predicted to form the a or p conformations, while the altered residues were mainly in the hydrophilic
Who reads Folding and Function of the Myelin Proteins from Primary Sequence Data?
It is typically read by researchers, students, and practitioners in Neuroscience.
- Author
- Dr. H. Inouye; Dr. D. A. Kirschner
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0360-4012)
- Published
- 1990
- Language
- EN
- Field
- Neuroscience (Life Sciences)