The role of hydrophobic amino acids at position 74 of DRB1 chain in rheumatoid arthritis

1994 ◽  
Vol 39 (2) ◽  
pp. 145
Author(s):  
M. Černá ◽  
E. Ivašková
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acids ◽  
Hydrophobic Amino Acids

A possible role of two hydrophobic amino acids in antigen recognition by synovial T cells in rheumatoid arthritis

1993 ◽  
Vol 23 (9) ◽  
pp. 2059-2065 ◽  
Author(s):  
Toshiaki Maruyama ◽  
Ichiro Saito ◽  
Sachiko Miyake ◽  
Hiroshi Hashimoto ◽  
Kazuto Sato ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acids ◽  
T Cells ◽  
Antigen Recognition ◽  
Hydrophobic Amino Acids

Role of Important Hydrophobic Amino Acids in the Interaction between the Glucocorticoid Receptor τ1-Core Activation Domain and Target Factors†

Biochemistry ◽  
1998 ◽  
Vol 37 (26) ◽  
pp. 9586-9594 ◽  
Author(s):  
Tova Almlöf ◽  
Annika E. Wallberg ◽  
Jan-Åke Gustafsson ◽  
Anthony P. H. Wright
Keyword(s):  
Amino Acids ◽  
Glucocorticoid Receptor ◽  
Activation Domain ◽  
Hydrophobic Amino Acids

scholarly journals Role of amino acids in rheumatoid arthritis studied by metabolomics

2017 ◽  
Vol 22 (1) ◽  
pp. 38-46 ◽  
Author(s):  
Min He ◽  
Amy C. Harms ◽  
Eduard van Wijk ◽  
Mei Wang ◽  
Ruud Berger ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acids

scholarly journals De Novo designed 13 mer hairpin-peptide arrests insulin and inhibits its aggregation: role of OH–π interactions between water and hydrophobic amino acids

RSC Advances ◽  
2020 ◽  
Vol 10 (25) ◽  
pp. 14991-14999
Author(s):  
Meghomukta Mukherjee ◽  
Nilanjan Banerjee ◽  
Subhrangsu Chatterjee
Keyword(s):  
Amino Acids ◽  
Neurodegenerative Diseases ◽  
Type Ii Diabetes ◽  
De Novo ◽  
Prion Diseases ◽  
Cellular Systems ◽  
Type Ii ◽  
P Protein ◽  
Hydrophobic Amino Acids

Protein aggregation in the cellular systems can be highly fatal causing a series of diseases including neurodegenerative diseases like ALS, Alzheimer, Prion Diseases, Parkinson's and other diseases like type II diabetes.

scholarly journals Role of Hydrophobic Amino Acids at β85 and β88 in Stabilizing F Helix Conformation of Hemoglobin S

1996 ◽  
Vol 271 (40) ◽  
pp. 24564-24568 ◽  
Author(s):  
Lattupally R. Reddy ◽  
Konda S. Reddy ◽  
Saul Surrey ◽  
Kazuhiko Adachi
Keyword(s):  
Amino Acids ◽  
Hemoglobin S ◽  
Hydrophobic Amino Acids ◽  
Helix Conformation

scholarly journals Role of conserved hydrophobic amino acids in androgen receptor AF-1 function

2003 ◽  
Vol 31 (3) ◽  
pp. 427-439 ◽  
Author(s):  
R Betney ◽  
IJ McEwan
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
Androgen Receptor ◽  
Gene Transcription ◽  
Hydrophobic Residues ◽  
Steroid Receptor Coactivator ◽  
Binding Interface ◽  
Hydrophobic Amino Acids

The intracellular androgen receptor (AR) is a ligand-activated transcription factor. Upon binding the steroids testosterone or dihydrotestosterone, the activated receptor translocates to the nucleus, binds to specific DNA response elements and interacts with the transcription machinery in order to regulate gene transcription. In the present study, we have described a highly conserved region (amino acids 224-258) within the AR AF-1 domain and have investigated the role of conserved bulky hydrophobic residues in gene regulation. Mutating pairs of residues (I229A/L236A; V240A/V242A; L251A/L254A) reduced transactivation activity by 25-40%. Mutating residues M244, L246 and V248 to alanines had a more dramatic affect on receptor activity, disrupting activity by at least 60%. The latter mutations also disrupted binding to the RNA polymerase-associated protein 74 subunit of the general transcription factor TFIIF. The protein conformation and stability of the mutant polypeptide in vitro was not significantly different from the wild type. None of the mutations tested disrupted binding of the AF-1 domain with the coactivator protein steroid receptor coactivator-1a. Thus we have concluded that conserved hydrophobic residues are important for receptor-dependent gene transcription and that M244, L246 and V248 are part of the binding interface for TFIIF.

scholarly journals Aggregation and Molecular Properties of β-Glucosidase Isoform II in Chayote (Sechium edule)

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1699
Author(s):  
Alberto Cruz Rodríguez ◽  
Fabiola Anaid Sánchez Esperanza ◽  
Eduardo Pérez-Campos ◽  
María Teresa Hernández-Huerta ◽  
Laura Pérez-Campos Mayoral ◽  
...  
Keyword(s):  
Amino Acids ◽  
Buffer Solution ◽  
Native Page ◽  
Sechium Edule ◽  
Chromatography Tandem Mass Spectrometry ◽  
Sds Page ◽  
Liquid Chromatography Tandem Mass ◽  
Hydrophobic Amino Acids ◽  
Nano Liquid Chromatography

The presence of isoforms of β-glucosidase has been reported in some grasses such as sorghum, rice and maize. This work aims to extract and characterize isoform II in β-glucosidase from S. edule. A crude extract was prepared without buffer solution and adjusted to pH 4.6. Contaminating proteins were precipitated at 4 °C for 24 h. The supernatant was purified by chromatography on carboxymethyl cellulose (CMC) column, molecular exclusion on Sephacryl S-200HR, and exchange anionic on QFF column. Electrophoretic analyzes revealed a purified enzyme with aggregating molecular complex on SDS-PAGE, Native-PAGE, and AU-PAGE. Twelve peptides fragments were identified by nano liquid chromatography-tandem mass spectrometry (nano LC-ESI-MS/MS), which presented as 61% identical to Cucurbita moschata β-glucosidase and 55.74% identical to β-glucosidase from Cucumis sativus, another Cucurbitaceous member. The relative masses which contained 39% hydrophobic amino acids ranged from 982.49 to 2,781.26. The enzyme showed a specificity to β-d-glucose with a Km of 4.59 mM, a Vmax value of 104.3 μM∙min−1 and a kcat of 10,087 μM∙min−1 using p-nitrophenyl-β-D-glucopyranoside. The presence of molecular aggregates can be attributed to non-polar amino acids. This property is not mediated by a β-glucosidase aggregating factor (BGAF) as in grasses (maize and sorghum). The role of these aggregates is discussed.

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