iHSP-PseRAAAC: Identifying the heat shock protein families using pseudo reduced amino acid alphabet composition

2013 ◽  
Vol 442 (1) ◽  
pp. 118-125 ◽  
Author(s):  
Peng-Mian Feng ◽  
Wei Chen ◽  
Hao Lin ◽  
Kuo-Chen Chou
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Families ◽  
Reduced Amino Acid Alphabet ◽  
Amino Acid Alphabet

Fast databank searching with a reduced amino-acid alphabet

1994 ◽  
Vol 10 (4) ◽  
pp. 453-454 ◽  
Author(s):  
Claudine Landès ◽  
Jean-Loup Risler
Keyword(s):  
Amino Acid ◽  
Reduced Amino Acid Alphabet ◽  
Amino Acid Alphabet

Purification of a mature form of 60kDa heat-shock protein (chaperonin homolog) from porcine kidney and its partial amino acid sequence

1992 ◽  
Vol 24 (9) ◽  
pp. 1507-1510 ◽  
Author(s):  
Wakui Hideki ◽  
Itoh Hideaki ◽  
Tashima Yohtalou ◽  
Kobayashi Ryoji ◽  
Nakamoto Yasushi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Porcine Kidney ◽  
Partial Amino Acid Sequence ◽  
Mature Form

Amino acid regions 357–368 and 418–427 of Streptococcus pyogenes 60kDa heat shock protein are recognized by antibodies from glaucomatous patient sera

2010 ◽  
Vol 48 (6) ◽  
pp. 239-244 ◽  
Author(s):  
Mario E. Cancino-Diaz ◽  
Martha Sanchez-Becerra ◽  
Celia Elizondo-Olascoaga ◽  
Sandra Rodríguez-Martínez ◽  
Juan C. Cancino-Diaz
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Streptococcus Pyogenes ◽  
Glaucomatous Patient

The expression of temperature-stress proteins in a desert cactus (Opuntia ficus indica)

Genome ◽  
1991 ◽  
Vol 34 (6) ◽  
pp. 940-943 ◽  
Author(s):  
Daryl J. Somers ◽  
Randal W. Giroux ◽  
W. Gary Filion
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Stress Proteins ◽  
Protein S ◽  
Protein Families ◽  
Opuntia Ficus Indica ◽  
Stress Acclimation ◽  
Molecular Masses ◽  
Shock Proteins

Opuntia ficus indica roots grown hydroponically at 20 or 30 °C were subjected to a range of heat-shock temperatures as high as 50 °C for 2 h. Roots grown at 30 °C sustained a greater level of total protein synthesis than did 20 °C-grown roots following heat-shock treatments ≥ 45 °C. The 30 °C-grown roots synthesized 31 families of heat-shock proteins between 38 and 47 °C in comparison with 20 °C-grown roots, which synthesized 19 families of heat-shock proteins at 45 °C. In both groups of roots, the heat-shock response was dominated equally by the 71–75 and a 62 kDa heat-shock protein families. In addition, the 20 °C-grown roots expressed 11 families of cold-shock proteins following 2 h at 4 °C, five of which had similar relative molecular masses to heat-shock protein families. There were numerous qualitative differences in the heat shock protein profiles between the roots grown at 20 and 30 °C; the 30 °C-grown roots expressed several unique heat shock protein families.Key words: heat-shock protein(s), cactus, thermal stress, acclimation.

scholarly journals Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain.

1990 ◽  
Vol 10 (3) ◽  
pp. 1234-1238 ◽  
Author(s):  
M A Stevenson ◽  
S K Calderwood
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Alpha Helix ◽  
Cellular Protein ◽  
Binding Domain ◽  
Functional Region ◽  
Amino Acid Homology ◽  
Calmodulin Binding ◽  
Essential Components

The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number cellular protein-protein interactions. We report here on the characterization of a new functional region in hsp70, a calmodulin-binding site. We have identified a 21-amino-acid sequence within the hsp70 protein that contains a calmodulin-binding domain. The peptide formed a potential amphipathic alpha helix and bound calmodulin with high affinity. Comparison of amino acid homology of this calmodulin-binding sequence with analogous hsp70 sequences from other species showed a high degree of conservation.

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