scholarly journals Mapping antibody binding sites on cytochrome c with synthetic peptides: Are results representative of the antigenic structure of proteins?

1993 ◽  
Vol 2 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Christian Schwab ◽  
Andrea Twardek ◽  
Hans Rudolf Bosshard ◽  
Terence P. Lo ◽  
Gary D. Brayer
Keyword(s):  
Cytochrome C ◽  
Binding Sites ◽  
Synthetic Peptides ◽  
Antibody Binding ◽  
Antigenic Structure ◽  
Structure Of Proteins

scholarly journals Two distinct binding sites for high potential iron-sulfur protein and cytochrome c on the reaction center-bound cytochrome of Rubrivivax gelatinosus.

2004 ◽  
Vol 279 (44) ◽  
pp. 46350
Author(s):  
Jean Alric ◽  
Makoto Yoshida ◽  
Kenji V.P. Nagashima ◽  
Rainer Hienerwadel ◽  
Pierre Parot ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Reaction Center ◽  
Binding Sites ◽  
High Potential ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Rubrivivax Gelatinosus

scholarly journals Identification of Immunodominant CD4-Restricted Epitopes Co-Located with Antibody Binding Sites in Individuals Vaccinated with ALVAC-HIV and AIDSVAX B/E

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0115582 ◽  
Author(s):  
Silvia Ratto-Kim ◽  
Mark S. de Souza ◽  
Jeffrey R. Currier ◽  
Nicos Karasavvas ◽  
John Sidney ◽  
...  
Keyword(s):  
Binding Sites ◽  
Antibody Binding

scholarly journals Localization of Antibody-Binding Sites by Sequence Analysis of Cloned Pilin Genes from Neisseria Gonorrhoeae

Microbiology ◽  
1987 ◽  
Vol 133 (4) ◽  
pp. 825-833 ◽  
Author(s):  
I. J. Nicolson ◽  
A. C. F. Perry ◽  
M. Virji ◽  
J. E. Heckels ◽  
J. R. Saunders
Keyword(s):  
Sequence Analysis ◽  
Neisseria Gonorrhoeae ◽  
Binding Sites ◽  
Antibody Binding

Global regulation of mitochondrial biogenesis in Saccharomyces cerevisiae: ABF1 and CPF1 play opposite roles in regulating expression of the QCR8 gene, which encodes subunit VIII of the mitochondrial ubiquinol-cytochrome c oxidoreductase

1992 ◽  
Vol 12 (6) ◽  
pp. 2872-2883
Author(s):  
J H de Winde ◽  
L A Grivell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Mitochondrial Biogenesis ◽  
Binding Sites ◽  
Promoter Region ◽  
S Phase ◽  
Negative Regulator ◽  
Global Regulation ◽  
Two Factors ◽  
Efficient Induction

The multifunctional DNA-binding proteins ABF1 and CPF1 bind in a mutually exclusive manner to the promoter region of the QCR8 gene, which encodes 11-kDa subunit VIII of the Saccharomyces cerevisiae mitochondrial ubiquinol-cytochrome c oxidoreductase (QCR). We investigated the roles that the two factors play in transcriptional regulation of this gene. To this end, the overlapping binding sites for ABF1 and CPF1 were mutated and placed in the chromosomal context of the QCR8 promoter. The effects on transcription of the QCR8 gene were analyzed both under steady-state conditions and during nutritional shifts. We found that ABF1 is required for repressed and derepressed transcription levels and for efficient induction of transcription upon escape from catabolite repression, independently of DNA replication. CPF1 acts as a negative regulator, modulating the overall induction response. Alleviation of repression through CPF1 requires passage through the S phase. Implications of these findings for the roles played by ABF1 and CPF1 in global regulation of mitochondrial biogenesis are discussed.

scholarly journals Molecular dynamics approach for capturing calixarenes--proteins interactions: the case of cytochrome c

2020 ◽  
Author(s):  
Alessio Bartocci ◽  
florence szczepaniak ◽  
Tao Jiang ◽  
Natacha Gillet ◽  
Elise Dumont
Keyword(s):  
Molecular Dynamics ◽  
Cytochrome C ◽  
Binding Sites ◽  
Supervised Machine Learning ◽  
Titration Calorimetry ◽  
X Ray ◽  
Poisson Boltzmann ◽  
Bond Network ◽  
Proteins Interactions ◽  
Detailed Picture

Here, we propose a molecular dynamics investigation of the supramolecular association of sulfonatedcalix-[8]-arenes to cytochrome c. The binding sites prone to interactions with sulfonated calixarenescan be identified without prior knowledge of the X-ray structure, and the binding free energiesestimated by molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) post-analysis arefound to be in neat agreement with the isothermal titration calorimetry (ITC) measurements The per-residuedecomposition reveals the detailed picture of this electrostatically-driven association and notably therole of the arginine R13 as a bridge residue between the two main anchoring sites. In addition,the analysis of the residue behavior by means of a supervised machine learning protocol unveils the formation of an hydrogen bond network far from the binding sites, increasing the rigidity of theprotein.

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