Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins
β Scribed by Susanne Moelbert; Eldon Emberly; Chao Tang
- Book ID
- 111752223
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2004
- Tongue
- English
- Weight
- 298 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0961-8368
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## Abstract Given the difficulty in determining highβresolution structures of helical membrane proteins, sequenceβbased prediction methods can be useful in elucidating diverse physiological processes mediated by this important class of proteins. Predicting the angular orientations of transmembrane
We examined the variation in the solvent accessibility and hydrophobicity of the amino acids along the sequences of 58 soluble globular proteins with known tertiary structure. We found that there is a significant tendency for the accessibilities to run in clusters along the sequence but that the hyd