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PMID: 1518784 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Hydrophobicity and structural classes in proteins.

Protein engineering ·Vol. 5 ·No. 5 ·1992-07-00 ·Pages 373-5

Cid H, Bunster M, Canales M, Gazitúa F

Abstract

The bulk hydrophobic character for the 20 natural amino acid residues, has been obtained from a database of 60 protein structures, grouped in the four structural classes alpha alpha, beta beta, alpha + beta and alpha/beta. The hydrophobicity coefficients thus obtained are compared with Ponnuswamy's original values using scales normalized to average = 0.0 and standard deviation = 1.0. Even though most of the amino acid residues do not change their hydropathic character in the different structural classes, their behaviour suggests the convenience that averaging methods should only consider proteins of the same structural class and that this information should be included in the secondary structure methods.

MeSH Terms
Amino Acids/chemistry Protein Conformation Proteins/chemistry,classification Structure-Activity Relationship
Chemicals
Amino Acids Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Cid H
Depto de Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Chile.
Bunster M
Canales M
Gazitúa F
Article Info
Journal
Protein engineering
Abbr.
Protein Eng
ISSN
0269-2139
Published
1992-07-00
Pages
373-5
Language
English
Region
England
NLM ID
8801484
Subset
IM
Analysis Services
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