The Optical Biosensor Studies on the Role of Hydrophobic Tails of NADPH-Cytochrome P450 Reductase and Cytochromes P450 2B4 and b5 upon Productive Complex Formation within a Monomeric Reconstituted System

Ivanov, Yuri D.; Kanaeva, Irina P.; Kuznetsov, Vadim Yu.; Lehnerer, Michael; Schulze, Johannes; Hlavica, Peter; Archakov, Alexander I.

doi:10.1006/abbi.1998.0981

Cited by 39 publications

(21 citation statements)

References 20 publications

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“…Recently, using fluorescence resonance energy transfer (FRET), Wang (65). The reason for the discrepancy in K D values that depends on the techniques for analyzing proteinprotein interactions is unclear.…”

Section: Single Turnover Reactions Of Heme Complexes Of Ho-1 Mutants-mentioning

confidence: 99%

Involvement of NADP(H) in the Interaction between Heme Oxygenase-1 and Cytochrome P450 Reductase

Higashimoto

Sakamoto

Hayashi

et al. 2005

Journal of Biological Chemistry

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Section: Single Turnover Reactions Of Heme Complexes Of Ho-1 Mutants-mentioning

confidence: 99%

Involvement of NADP(H) in the Interaction between Heme Oxygenase-1 and Cytochrome P450 Reductase

Higashimoto

Sakamoto

Hayashi

et al. 2005

Journal of Biological Chemistry

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“…The average value of the contact surface of monomers is about 800 Å 2 [12,13]. Analysis of these surfaces revealed an increase in the number of arginine, histidine, asparagine, tryptophan, tyrosine and serine [13,14] and hydrophobic amino acid residues [12,15,16].…”

Section: Protein-protein Contacts: Structure Composition and Forcesmentioning

confidence: 99%

“…Contribution of hydrophobic interaction is higher in permanent complexes than in temporary complexes [12]. However, the temporary complexes of membrane proteins, such as cytochrome P450 2B4, cytochrome b 5 , NADPH-specific flavoprotein in contrast to water soluble proteins, are formed by hydrophobic interaction of their membrane parts [15,16]. In the case of enzyme interaction with peptide inhibitors or substrates the contacted interfaces may have hydrophilic surfaces [12,21].…”

Section: Protein-protein Contacts: Structure Composition and Forcesmentioning

confidence: 99%

Protein‐protein interactions as a target for drugs in proteomics

et al. 2003

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Protein-protein interactions play a central role in numerous processes in the cell and are one of the main fields of functional proteomics. This review highlights the methods of bioinformatics and functional proteomics of protein-protein interaction investigation. The structures and properties of contact surfaces, forces involved in protein-protein interactions, kinetic and thermodynamic parameters of these reactions were considered. The properties of protein contact surfaces depend on their functions. The contact surfaces of permanent complexes resemble domain contacts or the protein core and it is reasonable to consider such complex formation as a continuation of protein folding. Characteristics of contact surfaces of temporary protein complexes share some similarities with active sites of enzymes. The contact surfaces of the temporary protein complexes have unique structure and properties and they are more conservative in comparison with active site of enzymes. So they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations were undertaken to find or design small molecules that block protein dimerization or protein(peptide)-receptor interaction, or, on the contrary, to induce protein dimerization.

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“…Of all biosensor types, particular attention should be paid to noncontact OBs that have found an ever-widening application in biology and medicine [54][55][56][57][58][59][60][61][62][63][64][65][66][67][68][69]. They are used in the real-time analyses of protein -protein interactions including the interactions between antigen/antibody, oligonucleotide/ oligonucleotide, protein/lipid, hormone/receptor and, also, drug/receptor -with the latter interactions being widely used for drug design and drug testing.…”

Section: Obsmentioning

confidence: 99%

Nanotechnologies in proteomics

Ivanov

Govorun

Быков³

et al. 2006

Proteomics

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Progress in proteomic researches is largely determined by development and implementation of new methods for the revelation and identification of proteins in biological material in a wide concentration range (from 10 23 M to single molecules). The most perspective approaches to address this problem involve (i) nanotechnological physicochemical procedures for the separation of multicomponent protein mixtures; among these of particular interest are biospecific nanotechnological procedures for selection of proteins from multicomponent protein mixtures with their subsequent concentration on solid support; (ii) identification and counting of single molecules by use of molecular detectors. The prototypes of biospecific nanotechnological procedures, based on the capture of ligand biomolecules by biomolecules of immobilized ligate and the concentration of the captured ligands on appropriate surfaces, are well known; these are affinity chromatography, magnetic biobeads technology, different biosensor methods, etc. Here, we review the most promising nanotechnological approaches for selection of proteins and kinetic characterization of their complexes based on these biospecific methods with subsequent MS/MS identification of proteins and protein complexes. Two major groups of methods for the analysis and identification of individual molecules and their complexes by use of molecular detectors will be reviewed: scanning probe microscopy (SPM) (including atomic-force microscopy) and cryomassdetector technology.

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The Optical Biosensor Studies on the Role of Hydrophobic Tails of NADPH-Cytochrome P450 Reductase and Cytochromes P450 2B4 and b5 upon Productive Complex Formation within a Monomeric Reconstituted System

Cited by 39 publications

References 20 publications

Involvement of NADP(H) in the Interaction between Heme Oxygenase-1 and Cytochrome P450 Reductase

Involvement of NADP(H) in the Interaction between Heme Oxygenase-1 and Cytochrome P450 Reductase

Protein‐protein interactions as a target for drugs in proteomics

Nanotechnologies in proteomics

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