Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (114)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Woodcock, S.
Right arrow Articles by Henrissat, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Woodcock, S.
Right arrow Articles by Henrissat, B.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering vol. 5 no. 7 pp. 629-635, 1992
© 1992 Oxford University Press


RESEARCH-ARTICLE

Detection of secondary structure elements in proteins by hydrophobic cluster analysis

Steve Woodcock, Jean-Paul Mornon1 and Bernard Henrissat2

Centre de Recherches sur les Macromolécules Végétales CNRS, BP 53X, F-38041 Grenoble, France 1Laboratoire de Minéralogie-Cristallographie, Départment des Macromolécules Biologiques. Universités Paris 6 et Paris 7, CNRS URA 09. Tour 16. 4 place Jussieu, F-75252 Paris cedex 05, France

2To whom correspondence should be addressed

Hydrophobic cluster analysis (HCA) is a protein sequence comparison method based on {alpha}-helical representations of the sequences where the size, shape and orientation of the clusters of hydrophobic residues are primarily compared. The effectiveness of HCA has been suggested to originate from its potential ability to focus on the residues forming the hydrophobic core of globular proteins. We have addressed the robustness of the bidimensional representation used for HCA in its ability to detect the regular secondary structure elements of proteins. Various parameters have been studied such as those governing cluster size and limits, the hydrophobic residues constituting the clusters as well as the potential shift of the cluster positions with respect to the position of the regular secondary structure elements. The following results have been found to support the {alpha}-helical bidimensional representation used in HCA: (i) there is a positive correlation (clearly above background noise) between the hydrophobic clusters and the regular secondary structure elements in proteins; (ii) the hydrophobic clusters are centred on the regular secondary structure elements; (iii) the pitch of the helical representation which gives the best correspondence is that of an {alpha}-helix. The correspondence between hydrophobic clusters and regular secondary structure elements suggests a way to implement variable gap penalties during the automatic alignment of protein sequences.

Keywords: computer analysis/helical nets/hydrophobic cluster analysis/secondary structure assignments

Received March 2, 1992; revised May 6, 1992; accepted July 16, 1992.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
A. E. Kister and I. Gelfand
Finding of residues crucial for supersecondary structure formation
PNAS, November 10, 2009; 106(45): 18996 - 19000.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
A. Gioti, J. M. Pradier, E. Fournier, P. Le Pecheur, C. Giraud, D. Debieu, J. Bach, P. Leroux, and C. Levis
A Botrytis cinerea Emopamil Binding Domain Protein, Required for Full Virulence, Belongs to a Eukaryotic Superfamily Which Has Expanded in Euascomycetes
Eukaryot. Cell, February 1, 2008; 7(2): 368 - 378.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
B. Ma, J. L. Simala-Grant, and D. E. Taylor
Fucosylation in prokaryotes and eukaryotes
Glycobiology, December 1, 2006; 16(12): 158R - 184R.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
C. Schmitt, L. Gouya, E. Malonova, J. Lamoril, J.-M. Camadro, M. Flamme, C. Rose, S. Lyoumi, V. Da Silva, C. Boileau, et al.
Mutations in human CPO gene predict clinical expression of either hepatic hereditary coproporphyria or erythropoietic harderoporphyria
Hum. Mol. Genet., October 15, 2005; 14(20): 3089 - 3098.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. Boulant, C. Vanbelle, C. Ebel, F. Penin, and J.-P. Lavergne
Hepatitis C Virus Core Protein Is a Dimeric Alpha-Helical Protein Exhibiting Membrane Protein Features
J. Virol., September 1, 2005; 79(17): 11353 - 11365.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
B. Neven, I. Callebaut, A.-M. Prieur, J. Feldmann, C. Bodemer, L. Lepore, B. Derfalvi, S. Benjaponpitak, R. Vesely, M. J. Sauvain, et al.
Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU
Blood, April 1, 2004; 103(7): 2809 - 2815.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
D. Znamenskiy, J. Chomilier, K. Le Tuan, and J.-P. Mornon
A new protein folding algorithm based on hydrophobic compactness: Rigid Unconnected Secondary Structure Iterative Assembly (RUSSIA). I: Methodology
Protein Eng. Des. Sel., December 1, 2003; 16(12): 925 - 935.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
I. Callebaut, D. Moshous, J.-P. Mornon, and J.-P. de Villartay
Metallo-{beta}-lactamase fold within nucleic acids processing enzymes: the {beta}-CASP family
Nucleic Acids Res., August 15, 2002; 30(16): 3592 - 3601.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
J.-S. Gatot, I. Callebaut, C. Van Lint, D. Demonte, P. Kerkhofs, D. Portetelle, A. Burny, L. Willems, and R. Kettmann
Bovine Leukemia Virus SU Protein Interacts with Zinc, and Mutations within Two Interacting Regions Differently Affect Viral Fusion and Infectivity In Vivo
J. Virol., July 17, 2002; 76(16): 7956 - 7967.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. H. Hassan, C. Wirblich, M. Forzan, and P. Roy
Expression and Functional Characterization of Bluetongue Virus VP5 Protein: Role in Cellular Permeabilization
J. Virol., September 15, 2001; 75(18): 8356 - 8367.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
P Bouchard, J Chomilier, V Ravet, J. Mornon, and B Vigues
Molecular characterization of the major membrane skeletal protein in the ciliate Tetrahymena pyriformis suggests n-plication of an early evolutionary intermediate filament protein subdomain
J. Cell Sci., January 1, 2001; 114(1): 101 - 110.
[Abstract] [PDF]


Home page
Mol. Endocrinol.Home page
R. Métivier, F. G. Petit, Y. Valotaire, and F. Pakdel
Function of N-Terminal Transactivation Domain of the Estrogen Receptor Requires a Potential {alpha}-Helical Structure and Is Negatively Regulated by the A Domain
Mol. Endocrinol., November 1, 2000; 14(11): 1849 - 1871.
[Abstract] [Full Text]


Home page
Hum Mol GenetHome page
P. Durand, S. Fabrega, B. Henrissat, J.-P. Mornon, and P. Lehn
Structural features of normal and mutant human lysosomal glycoside hydrolases deduced from bioinformatics analysis
Hum. Mol. Genet., April 1, 2000; 9(6): 967 - 977.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. J. Bertram, N. G. Berube, X. Hang-Swanson, Q. Ran, J. K. Leung, S. Bryce, K. Spurgers, R. J. Bick, A. Baldini, Y. Ning, et al.
Identification of a Gene That Reverses the Immortal Phenotype of a Subset of Cells and Is a Member of a Novel Family of Transcription Factor-Like Genes
Mol. Cell. Biol., February 1, 1999; 19(2): 1479 - 1485.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J.-S. Gatot, I. Callebaut, J.-P. Mornon, D. Portetelle, A. Burny, P. Kerkhofs, R. Kettmann, and L. Willems
Conservative Mutations in the Immunosuppressive Region of the Bovine Leukemia Virus Transmembrane Protein Affect Fusion but Not Infectivity in Vivo
J. Biol. Chem., May 22, 1998; 273(21): 12870 - 12880.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Q. Ye, I. Callebaut, A. Pezhman, J.-C. Courvalin, and H. J. Worman
Domain-specific Interactions of Human HP1-type Chromodomain Proteins and Inner Nuclear Membrane Protein LBR
J. Biol. Chem., June 6, 1997; 272(23): 14983 - 14989.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Eyries, A. Michaud, J. Deinum, M. Agrapart, J. Chomilier, C. Kramers, and F. Soubrier
Increased Shedding of Angiotensin-converting Enzyme by a Mutation Identified in the Stalk Region
J. Biol. Chem., February 16, 2001; 276(8): 5525 - 5532.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.