Abstract
This chapter describes the use of routines for plotting hydrophobicity, charge, and hydrophobic moments, drawing helix wheels and predicting secondary structure. Use of all these routines is very straightforward, and they are contained in the program PIP.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105–132.
Eisenberg, D., Schwarz, E. Komaromy, M., and Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125–142.
Schiffer, M. and Edmundson, A. B. (1967) Use of helical wheels to represent the structures of proteins and to identify the segments with helical potential. Biophys. J. 7, 121–135.
Gamier, J., Osguthorpe, D J, and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins J Mol Biol. 120, 97–120.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1994 Human Press Inc, Totowa, NJ
About this protocol
Cite this protocol
Staden, R. (1994). Staden: Statistical and Structural Analysis of Protein Sequences. In: Computer Analysis of Sequence Data. Methods in Molecular Biology, vol 25. Springer, Totowa, NJ. https://doi.org/10.1385/0-89603-276-0:125
Download citation
DOI: https://doi.org/10.1385/0-89603-276-0:125
Publisher Name: Springer, Totowa, NJ
Print ISBN: 978-0-89603-276-7
Online ISBN: 978-1-59259-512-9
eBook Packages: Springer Protocols