NDLI: Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues.

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Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues.

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Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	King, J. Schwartz, R. Istrail, S.
Description	Country affiliation: United States Author Affiliation: Schwartz R ( Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.)
Abstract	Patterns of hydrophobic and hydrophilic residues play a major role in protein folding and function. Long, predominantly hydrophobic strings of 20-22 amino acids each are associated with transmembrane helices and have been used to identify such sequences. Much less attention has been paid to hydrophobic sequences within globular proteins. In prior work on computer simulations of the competition between on-pathway folding and off-pathway aggregate formation, we found that long sequences of consecutive hydrophobic residues promoted aggregation within the model, even controlling for overall hydrophobic content. We report here on an analysis of the frequencies of different lengths of contiguous blocks of hydrophobic residues in a database of amino acid sequences of proteins of known structure. Sequences of three or more consecutive hydrophobic residues are found to be significantly less common in actual globular proteins than would be predicted if residues were selected independently. The result may reflect selection against long blocks of hydrophobic residues within globular proteins relative to what would be expected if residue hydrophobicities were independent of those of nearby residues in the sequence.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids Metabolism Computational Biology Plant Proteins Protein Folding Proteins Chemistry Alkyl And Aryl Transferases Animals Caenorhabditis Elegans Computer Simulation Cytidine Deaminase Databases As Topic Escherichia Coli Geranyltranstransferase Lipase Models, Molecular Oxidoreductases Acting On Ch-nh Group Donors Probability Protein Conformation Saccharomyces Cerevisiae Udpglucose-hexose-1-phosphate Uridylyltransferase Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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