l-Lysine and l-arginine inhibit myosin aggregation and interact with acidic amino acid residues of myosin: The role in increasing myosin solubility

2018 ◽  
Vol 242 ◽  
pp. 22-28 ◽  
Author(s):  
Shiyi Li ◽  
Yadong Zheng ◽  
Peng Xu ◽  
Xiaoxu Zhu ◽  
Cunliu Zhou
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

Involvement of Acidic Amino Acid Residues in Zn2+Binding to Respiratory Complex I

ChemBioChem ◽  
2015 ◽  
Vol 16 (14) ◽  
pp. 2080-2085 ◽  
Author(s):  
Sébastien Kriegel ◽  
Batoul Srour ◽  
Stefan Steimle ◽  
Thorsten Friedrich ◽  
Petra Hellwig
Keyword(s):  
Amino Acid ◽  
Complex I ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Respiratory Complex ◽  
Respiratory Complex I

scholarly journals Role of Integrase in Reverse Transcription of the Saccharomyces cerevisiae Retrotransposon Ty1

2005 ◽  
Vol 4 (6) ◽  
pp. 1057-1065 ◽  
Author(s):  
M. Wilhelm ◽  
F.-X. Wilhelm
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Specific Activity ◽  
Rnase H ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Acidic Domain ◽  
Basic Region

ABSTRACT Reverse transcriptase (RT) with its associated RNase H (RH) domain and integrase (IN) are key enzymes encoded by retroviruses and retrotransposons. Several studies have implied a functional role of the interaction between IN and RT during the replication of retroviral and retrotransposon genomes. In this study, IN deletion mutants were used to investigate the role of IN on the RT activity of the yeast Saccharomyces cerevisiae retrotransposon Ty1. We have identified two domains of Ty1 integrase which have effects on RT activity in vivo. The deletion of a domain spanning amino acid residues 233 to 520 of IN increases the exogenous specific activity of RT up to 20-fold, whereas the removal of a region rich in acidic amino acid residues between residues 521 and 607 decreases its activity. The last result complements our observation that an active recombinant RT protein can be obtained if a small acidic tail mimicking the acidic domain of IN is fused to the RT-RH domain. We suggest that interaction between these acidic amino acid residues of IN and a basic region of RT could be critical for the correct folding of RT and for the formation of an active conformation of the enzyme.

scholarly journals Conserved Acidic Amino Acid Residues in a Second RNA Recognition Motif Regulate Assembly and Function of TDP-43

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e52776 ◽  
Author(s):  
Akemi Shodai ◽  
Akemi Ido ◽  
Noriko Fujiwara ◽  
Takashi Ayaki ◽  
Toshifumi Morimura ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Recognition Motif ◽  
And Function

Electron Transfer Reaction of Glucose Oxidase Hybrids Modified with PhenothiazineviaPoly(ethylene oxide) Spacer on Acidic Amino Acid Residues

2002 ◽  
Vol 31 (2) ◽  
pp. 256-257 ◽  
Author(s):  
Sayuri Aoki ◽  
Kunikazu Ishii ◽  
Takeshi Ueki ◽  
Kazumichi Ban ◽  
Shin-ichiro Imabayashi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Ethylene Oxide ◽  
Glucose Oxidase ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

scholarly journals Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies

1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S R Patanjali ◽  
M J Swamy ◽  
A Surolia
Keyword(s):  
Amino Acid ◽  
Protein A ◽  
Stopped Flow ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Native Protein ◽  
Tryptophan Residues ◽  
Stopped Flow Kinetics ◽  
Two Phases ◽  
Kinetics Of

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

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