scholarly journals Order in Disorder as Observed by the “Hydrophobic Cluster Analysis” of Protein Sequences

PROTEOMICS ◽  
2018 ◽  
Vol 18 (21-22) ◽  
pp. 1800054 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Alexis Lamiable ◽  
Jean-Paul Mornon ◽  
Isabelle Callebaut
Keyword(s):  
Cluster Analysis ◽  
Protein Sequences ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster

Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences

Biochimie ◽  
1990 ◽  
Vol 72 (8) ◽  
pp. 555-574 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
B. Henrissat ◽  
C. Gaboriaud ◽  
V. Bissery ◽  
A. Morgat ◽  
...  
Keyword(s):  
Cluster Analysis ◽  
Protein Sequences ◽  
Functional Information ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster

scholarly journals Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins

1988 ◽  
Vol 255 (3) ◽  
pp. 901-905 ◽  
Author(s):  
B Henrissat ◽  
Y Popineau ◽  
J C Kader
Keyword(s):  
Cluster Analysis ◽  
Storage Proteins ◽  
Spinacia Oleracea ◽  
Protein Sequences ◽  
Protein Chain ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Conserved Domains ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.

Visualization of Protein Sequences Using the Two-Dimensional Hydrophobic Cluster Analysis Method

1995 ◽  
pp. 129-144
Author(s):  
Michel T. Semertzidis ◽  
Etienne Thoreau ◽  
Anne Tasso ◽  
Bernard Henrissat ◽  
Isabelle Callebaut ◽  
...  
Keyword(s):  
Cluster Analysis ◽  
Protein Sequences ◽  
Two Dimensional ◽  
Analysis Method ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster ◽  
Cluster Analysis Method

scholarly journals HCAtk and pyHCA: A Toolkit and Python API for the Hydrophobic Cluster Analysis of Protein Sequences

2018 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Isabelle Callebaut
Keyword(s):  
Cluster Analysis ◽  
Protein Domains ◽  
Protein Sequences ◽  
Command Line ◽  
Challenging Problem ◽  
Hydrophobic Cluster Analysis ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Hydrophobic Cluster ◽  
Link Type

AbstractMotivation: Detecting protein domains sharing no similarity to known domains, as stored in domain databases, is a challenging problem, particularly for unannotated proteomes, domains emerged recently, fast diverging proteins or domains with intrinsically disordered regions.Results: We developed pyHCA and HCAtk, a python API and standalone tool gathering together improved versions of previously developed methodologies, with new functionalities. The developed tools can be either used from command line or from a python API.Availability: HCAtk and pyHCA are available at https://github.com/T-B-F/pyHCA under the CeCILL-C license.

MANSEK and SUNHCA. Two interactive programs for the hydrophobic cluster analysis of protein sequences

1993 ◽  
Vol 9 (1) ◽  
pp. 37-44 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
C. Gaboriaud ◽  
A. Morgat ◽  
G. Pantel ◽  
J. P. Mornon ◽  
...  
Keyword(s):  
Cluster Analysis ◽  
Protein Sequences ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster

scholarly journals Identification of the catalytic residues of the first family of β(1–3)glucanosyltransferases identified in fungi

2000 ◽  
Vol 347 (3) ◽  
pp. 741-747 ◽  
Author(s):  
Isabelle MOUYNA ◽  
Michel MONOD ◽  
Thierry FONTAINE ◽  
Bernard HENRISSAT ◽  
Barbara LÉCHENNE ◽  
...  
Keyword(s):  
Cluster Analysis ◽  
Active Site ◽  
Biochemical Analysis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Sequence Comparisons ◽  
Catalytic Residues ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster ◽  
New Family

A new family of glycosylphosphatidylinositol-anchored β(1-3)glucanosyltransferases (Gelp), recently identified and characterized in the filamentous fungus Aspergillus fumigatus, showed functional similarity to the Gas/Phr/Epd protein families, which are involved in yeast morphogenesis. Sequence comparisons and hydrophobic cluster analysis (HCA) showed that all the Gas/Phr/Epd/Gel proteins belong to a new family of glycosylhydrolases, family 72. We confirmed by site-directed mutagenesis and biochemical analysis that the two conserved glutamate residues (the putative catalytic residues of this family, as determined by HCA) are involved in the active site of this family of glycosylhydrolases.

Hydrophobic Cluster Analysis Reveals a Third Chromodomain in theTetrahymenaPdd1p Protein of the Chromo Superfamily

1997 ◽  
Vol 235 (1) ◽  
pp. 103-107 ◽  
Author(s):  
Isabelle Callebaut ◽  
Jean-Claude Courvalin ◽  
Howard J. Worman ◽  
Jean-Paul Mornon
Keyword(s):  
Cluster Analysis ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster
Sign in / Sign up

Export Citation Format

Share Document