Pub Date : 2011-01-01Epub Date: 2011-03-20DOI: 10.1155/2011/579402
T A Karelina, H Ma, I Goryanin, O V Demin
The mathematical model of the operation of the first enzyme of the Escherichia coli phosphotransferase system, EI, is proposed. Parameters of the kinetic model describing the operation of EI under different conditions are identified on the basis of a large amount of known experimental data. The verified model is employed to predict modes of operation of EI under both in vivo physiological conditions and in vitro nonphysiological conditions. The model predicts that under in vivo physiological conditions, the rate of phosphotransfer from EI to the second protein of the phosphotransferase system HPr by the dimer is much higher than by the monomer. A hypothesis is proposed on the basis of calculations that the transfer by a monomer plays a role in the regulation of chemotaxis. At submicromolar pyruvate concentration, the model predicts nonmonotonic dependence of the phosphotransfer rate on the substrate (PEP) concentration.
{"title":"EI of the Phosphotransferase System of Escherichia coli: Mathematical Modeling Approach to Analysis of Its Kinetic Properties.","authors":"T A Karelina, H Ma, I Goryanin, O V Demin","doi":"10.1155/2011/579402","DOIUrl":"https://doi.org/10.1155/2011/579402","url":null,"abstract":"<p><p>The mathematical model of the operation of the first enzyme of the Escherichia coli phosphotransferase system, EI, is proposed. Parameters of the kinetic model describing the operation of EI under different conditions are identified on the basis of a large amount of known experimental data. The verified model is employed to predict modes of operation of EI under both in vivo physiological conditions and in vitro nonphysiological conditions. The model predicts that under in vivo physiological conditions, the rate of phosphotransfer from EI to the second protein of the phosphotransferase system HPr by the dimer is much higher than by the monomer. A hypothesis is proposed on the basis of calculations that the transfer by a monomer plays a role in the regulation of chemotaxis. At submicromolar pyruvate concentration, the model predicts nonmonotonic dependence of the phosphotransfer rate on the substrate (PEP) concentration.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2011 ","pages":"579402"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/579402","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30277864","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2011-01-01Epub Date: 2011-08-17DOI: 10.1155/2011/290617
R M Dünki, M Dressel
Reducing a feature vector to an optimized dimensionality is a common problem in biomedical signal analysis. This analysis retrieves the characteristics of the time series and its associated measures with an adequate methodology followed by an appropriate statistical assessment of these measures (e.g., spectral power or fractal dimension). As a step towards such a statistical assessment, we present a data resampling approach. The techniques allow estimating σ(2)(F), that is, the variance of an F-value from variance analysis. Three test statistics are derived from the so-called F-ratio σ(2)(F)/F(2). A Bayesian formalism assigns weights to hypotheses and their corresponding measures considered (hypothesis weighting). This leads to complete, partial, or noninclusion of these measures into an optimized feature vector. We thus distinguished the EEG of healthy probands from the EEG of patients diagnosed as schizophrenic. A reliable discriminance performance of 81% based on Taken's χ, α-, and δ-power was found.
{"title":"F-ratio test and hypothesis weighting: a methodology to optimize feature vector size.","authors":"R M Dünki, M Dressel","doi":"10.1155/2011/290617","DOIUrl":"https://doi.org/10.1155/2011/290617","url":null,"abstract":"<p><p>Reducing a feature vector to an optimized dimensionality is a common problem in biomedical signal analysis. This analysis retrieves the characteristics of the time series and its associated measures with an adequate methodology followed by an appropriate statistical assessment of these measures (e.g., spectral power or fractal dimension). As a step towards such a statistical assessment, we present a data resampling approach. The techniques allow estimating σ(2)(F), that is, the variance of an F-value from variance analysis. Three test statistics are derived from the so-called F-ratio σ(2)(F)/F(2). A Bayesian formalism assigns weights to hypotheses and their corresponding measures considered (hypothesis weighting). This leads to complete, partial, or noninclusion of these measures into an optimized feature vector. We thus distinguished the EEG of healthy probands from the EEG of patients diagnosed as schizophrenic. A reliable discriminance performance of 81% based on Taken's χ, α-, and δ-power was found.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2011 ","pages":"290617"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/290617","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29956405","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The baseplate subantenna in chlorosomes of green anoxygenic photosynthetic bacteria, belonging to the families Chloroflexaceae and Chlorobiaceae, is known to represent a complex of bacteriochlorophyll (BChl) a with the ~6 kDa CsmA proteins. Earlier, we showed the existence of a similar BChl a subantenna in chlorosomes of the photosynthetic green bacterium Oscillochloris trichoides, member of Oscillochloridaceae, the third family of green photosynthetic bacteria. However, this BChl a subantenna was not visually identified in absorption spectra of isolated Osc. trichoides chlorosomes in contrast to those of Chloroflexaceae and Chlorobiaceae. In this work, using room and low-temperature absorbance and fluorescence spectroscopy and sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis of alkaline-treated and untreated chlorosomes of Osc. trichoides, we showed that the baseplate BChl a subantenna does exist in Oscillochloridaceae chlorosomes as a complex of BChl a with the 5.7 kDa CsmA protein. The present results support the idea that the baseplate subantenna, representing a complex of BChl a with a ~6 kDa CsmA protein, is a universal interface between the BChl c subantenna of chlorosomes and the nearest light-harvesting BChl a subantenna in all three known families of green anoxygenic photosynthetic bacteria.
{"title":"CsmA Protein is Associated with BChl a in the Baseplate Subantenna of Chlorosomes of the Photosynthetic Green Filamentous Bacterium Oscillochloris trichoides belonging to the Family Oscillochloridaceae.","authors":"Anastasiya Zobova, Alexandra Taisova, Eugeny Lukashev, Nataliya Fedorova, Ludmila Baratova, Zoya Fetisova","doi":"10.1155/2011/860382","DOIUrl":"https://doi.org/10.1155/2011/860382","url":null,"abstract":"<p><p>The baseplate subantenna in chlorosomes of green anoxygenic photosynthetic bacteria, belonging to the families Chloroflexaceae and Chlorobiaceae, is known to represent a complex of bacteriochlorophyll (BChl) a with the ~6 kDa CsmA proteins. Earlier, we showed the existence of a similar BChl a subantenna in chlorosomes of the photosynthetic green bacterium Oscillochloris trichoides, member of Oscillochloridaceae, the third family of green photosynthetic bacteria. However, this BChl a subantenna was not visually identified in absorption spectra of isolated Osc. trichoides chlorosomes in contrast to those of Chloroflexaceae and Chlorobiaceae. In this work, using room and low-temperature absorbance and fluorescence spectroscopy and sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis of alkaline-treated and untreated chlorosomes of Osc. trichoides, we showed that the baseplate BChl a subantenna does exist in Oscillochloridaceae chlorosomes as a complex of BChl a with the 5.7 kDa CsmA protein. The present results support the idea that the baseplate subantenna, representing a complex of BChl a with a ~6 kDa CsmA protein, is a universal interface between the BChl c subantenna of chlorosomes and the nearest light-harvesting BChl a subantenna in all three known families of green anoxygenic photosynthetic bacteria.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2011 ","pages":"860382"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/860382","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30016891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ampullosporin A is an antimicrobial, neuroleptic peptaibol, the behavior of which was investigated in different membrane mimetic environments made of egg yolk L-α-phosphatidylcholine. In monolayers, the peptaibol adopted a mixed α/3(10)-helical structure with an in-plane orientation. The binding step was followed by the peptide insertion into the lipid monolayer core. The relevance of the inner lipid leaflet nature was studied by comparing ampullosporin binding on a hybrid bilayer, in which this leaflet was a rigid alkane layer, and on supported fluid lipid bilayers. The membrane binding was examined by surface plasmon resonance spectroscopy and the effect on lipid dynamics was explored using fluorescence recovery after photobleaching. In the absence of voltage and at low concentration, ampullosporin A substantially adsorbed onto lipid surfaces and its interaction with biomimetic models was strongly modified depending on the inner leaflet structure. At high concentration, ampullosporin A addition led to the lipid bilayers disruption.
安普霉素 A 是一种抗菌剂、神经抑制剂,研究人员对其在蛋黄 L-α-磷脂酰胆碱制成的不同膜模拟环境中的行为进行了研究。在单层膜中,七叶皂苷呈平面内取向的α/3(10)螺旋混合结构。结合步骤之后,肽插入单层脂质核心。通过比较安普霉素在混合双分子层(其中小叶为刚性烷烃层)和支撑流体脂质双分子层上的结合情况,研究了内部脂质小叶性质的相关性。通过表面等离子体共振光谱分析了膜结合情况,并利用光漂白后的荧光恢复探索了对脂质动态的影响。在无电压和低浓度的情况下,安普洛霉素 A 可大量吸附在脂质表面,其与生物仿真模型的相互作用因内部小叶结构的不同而发生强烈变化。在高浓度下,加入安普霉素 A 会导致脂质双层膜破坏。
{"title":"Exploring the membrane mechanism of the bioactive peptaibol ampullosporin a using lipid monolayers and supported biomimetic membranes.","authors":"Marguerita Eid, Sonia Rippa, Sabine Castano, Bernard Desbat, Joël Chopineau, Claire Rossi, Laure Béven","doi":"10.1155/2010/179641","DOIUrl":"10.1155/2010/179641","url":null,"abstract":"<p><p>Ampullosporin A is an antimicrobial, neuroleptic peptaibol, the behavior of which was investigated in different membrane mimetic environments made of egg yolk L-α-phosphatidylcholine. In monolayers, the peptaibol adopted a mixed α/3(10)-helical structure with an in-plane orientation. The binding step was followed by the peptide insertion into the lipid monolayer core. The relevance of the inner lipid leaflet nature was studied by comparing ampullosporin binding on a hybrid bilayer, in which this leaflet was a rigid alkane layer, and on supported fluid lipid bilayers. The membrane binding was examined by surface plasmon resonance spectroscopy and the effect on lipid dynamics was explored using fluorescence recovery after photobleaching. In the absence of voltage and at low concentration, ampullosporin A substantially adsorbed onto lipid surfaces and its interaction with biomimetic models was strongly modified depending on the inner leaflet structure. At high concentration, ampullosporin A addition led to the lipid bilayers disruption.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2010 ","pages":"179641"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042626/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29741049","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2010-01-01Epub Date: 2010-04-07DOI: 10.1155/2010/253763
M Gantri, H Trabelsi, E Sediki, R Ben Salah
We present a numerical spectroscopic study of visible and infrared laser radiation in a biological tissue. We derive a solution of a general two-dimensional time dependent radiative transfer equation in a tissue-like medium. The used model is suitable for many situations especially when the external source is time-dependent or continuous. We use a control volume-discrete ordinate method associated with an implicit three-level second-order time differencing scheme. We consider a very thin rectangular biological-tissue-like medium submitted to a visible or a near infrared light sources. The RTE is solved for a set of different wavelength source. All sources are assumed to be monochromatic and collimated. The energetic fluence rate is computed at a set of detector points on the boundaries. According to the source type, we investigate either the steady-state or transient response of the medium. The used model is validated in the case of a heterogeneous tissue-like medium using referencing experimental results from the literature. Also, the developed model is used to study changes on transmitted light in a rat-liver tissue-like medium. Optical properties depend on the source wavelength and they are taken from the literature. In particular, light-transmission in the medium is studied for continuous wave and for short pulse.
{"title":"Computational laser spectroscopy in a biological tissue.","authors":"M Gantri, H Trabelsi, E Sediki, R Ben Salah","doi":"10.1155/2010/253763","DOIUrl":"https://doi.org/10.1155/2010/253763","url":null,"abstract":"<p><p>We present a numerical spectroscopic study of visible and infrared laser radiation in a biological tissue. We derive a solution of a general two-dimensional time dependent radiative transfer equation in a tissue-like medium. The used model is suitable for many situations especially when the external source is time-dependent or continuous. We use a control volume-discrete ordinate method associated with an implicit three-level second-order time differencing scheme. We consider a very thin rectangular biological-tissue-like medium submitted to a visible or a near infrared light sources. The RTE is solved for a set of different wavelength source. All sources are assumed to be monochromatic and collimated. The energetic fluence rate is computed at a set of detector points on the boundaries. According to the source type, we investigate either the steady-state or transient response of the medium. The used model is validated in the case of a heterogeneous tissue-like medium using referencing experimental results from the literature. Also, the developed model is used to study changes on transmitted light in a rat-liver tissue-like medium. Optical properties depend on the source wavelength and they are taken from the literature. In particular, light-transmission in the medium is studied for continuous wave and for short pulse.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2010 ","pages":"253763"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2010/253763","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28925695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-01-01Epub Date: 2009-10-18DOI: 10.1155/2009/380976
T C A Molteno, W L Kennedy
A quantitative frequency-domain model of induction-based magnetoreception is presented for elasmobranch fishes. We show that orientation with respect to the geomagnetic field can be determined by synchronous detection of electrosensory signals at harmonics of the vestibular frequency. The sensitivity required for this compass-sense mechanism is shown to be less than that known from behavioral experiments. Recent attached-magnet experiments have called into doubt the induction-based mechanism for magnetoreception. We show that the use of attached magnets would interfere with an induction-based mechanism unless relative movement between the electrosensory system and the attached magnet is less than 100 mum. This suggests that further experiments may be required to eliminate induction as a basis for magnetoreception.
{"title":"Navigation by induction-based magnetoreception in elasmobranch fishes.","authors":"T C A Molteno, W L Kennedy","doi":"10.1155/2009/380976","DOIUrl":"https://doi.org/10.1155/2009/380976","url":null,"abstract":"<p><p>A quantitative frequency-domain model of induction-based magnetoreception is presented for elasmobranch fishes. We show that orientation with respect to the geomagnetic field can be determined by synchronous detection of electrosensory signals at harmonics of the vestibular frequency. The sensitivity required for this compass-sense mechanism is shown to be less than that known from behavioral experiments. Recent attached-magnet experiments have called into doubt the induction-based mechanism for magnetoreception. We show that the use of attached magnets would interfere with an induction-based mechanism unless relative movement between the electrosensory system and the attached magnet is less than 100 mum. This suggests that further experiments may be required to eliminate induction as a basis for magnetoreception.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2009 ","pages":"380976"},"PeriodicalIF":0.0,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2009/380976","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28692658","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-01-01Epub Date: 2010-02-04DOI: 10.1155/2009/210485
Shagufta H Khan, Raj Kumar
A number of proteins with intrinsically disordered (ID) regions/domains are reported to be found disproportionately higher in transcription factors. Available evidences suggest that presence of ID region/domain within a transcription factor plays an important role in its biological functions. These ID sequences provide large flexible surfaces that can allow them to make more efficient physical and functional interactions with their target partners. Since transcription factors regulate expression of target genes by interacting with specific coregulatory proteins, these ID regions/domains can be used as a platform for such large macromolecular interactions, and may represent a mechanism for regulation of cellular processes. The precise structural basis for the function of these ID regions/domains of the transcription factors remains to be determined. In the recent years there has been growing evidence suggesting that an induced fit-like process leads to imposition of folded functional structure in these ID domains on which large multiprotein complexes are built. These multiprotein complexes may eventually dictate the final outcome of the gene regulation by the transcription factors.
{"title":"An overview of the importance of conformational flexibility in gene regulation by the transcription factors.","authors":"Shagufta H Khan, Raj Kumar","doi":"10.1155/2009/210485","DOIUrl":"https://doi.org/10.1155/2009/210485","url":null,"abstract":"<p><p>A number of proteins with intrinsically disordered (ID) regions/domains are reported to be found disproportionately higher in transcription factors. Available evidences suggest that presence of ID region/domain within a transcription factor plays an important role in its biological functions. These ID sequences provide large flexible surfaces that can allow them to make more efficient physical and functional interactions with their target partners. Since transcription factors regulate expression of target genes by interacting with specific coregulatory proteins, these ID regions/domains can be used as a platform for such large macromolecular interactions, and may represent a mechanism for regulation of cellular processes. The precise structural basis for the function of these ID regions/domains of the transcription factors remains to be determined. In the recent years there has been growing evidence suggesting that an induced fit-like process leads to imposition of folded functional structure in these ID domains on which large multiprotein complexes are built. These multiprotein complexes may eventually dictate the final outcome of the gene regulation by the transcription factors.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2009 ","pages":"210485"},"PeriodicalIF":0.0,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2009/210485","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28723406","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-01-01Epub Date: 2009-10-13DOI: 10.1155/2009/380967
Masataka Kawai, Xiaoying Lu, Sarah E Hitchcock-Degregori, Kristen J Stanton, Michael W Wandling
Tropomyosin (Tm) consists of 7 quasiequivalent repeats known as "periods," and its specific function may be associated with these periods. To test the hypothesis that either period 2 or 3 promotes force generation by inducing a positive allosteric effect on actin, we reconstituted the thin filament with mutant Tm in which either period 2 (Delta2Tm) or period 3 (Delta3Tm) was deleted. We then studied: isometric tension, stiffness, 6 kinetic constants, and the pCa-tension relationship. N-terminal acetylation of Tm did not cause any differences. The isometric tension in Delta2Tm remained unchanged, and was reduced to approximately 60% in Delta3Tm. Although the kinetic constants underwent small changes, the occupancy of strongly attached cross-bridges was not much different. The Hill factor (cooperativity) did not differ significantly between Delta2Tm (1.79 +/- 0.19) and the control (1.73 +/- 0.21), or Delta3Tm (1.35 +/- 0.22) and the control. In contrast, pCa(50) decreased slightly in Delta2Tm (5.11 +/- 0.07), and increased significantly in Delta3Tm (5.57 +/- 0.09) compared to the control (5.28 +/- 0.04). These results demonstrate that, when ions are present at physiological concentrations in the muscle fiber system, period 3 (but not period 2) is essential for the positive allosteric effect that enhances the interaction between actin and myosin, and increases isometric force of each cross-bridge.
{"title":"Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.","authors":"Masataka Kawai, Xiaoying Lu, Sarah E Hitchcock-Degregori, Kristen J Stanton, Michael W Wandling","doi":"10.1155/2009/380967","DOIUrl":"https://doi.org/10.1155/2009/380967","url":null,"abstract":"<p><p>Tropomyosin (Tm) consists of 7 quasiequivalent repeats known as \"periods,\" and its specific function may be associated with these periods. To test the hypothesis that either period 2 or 3 promotes force generation by inducing a positive allosteric effect on actin, we reconstituted the thin filament with mutant Tm in which either period 2 (Delta2Tm) or period 3 (Delta3Tm) was deleted. We then studied: isometric tension, stiffness, 6 kinetic constants, and the pCa-tension relationship. N-terminal acetylation of Tm did not cause any differences. The isometric tension in Delta2Tm remained unchanged, and was reduced to approximately 60% in Delta3Tm. Although the kinetic constants underwent small changes, the occupancy of strongly attached cross-bridges was not much different. The Hill factor (cooperativity) did not differ significantly between Delta2Tm (1.79 +/- 0.19) and the control (1.73 +/- 0.21), or Delta3Tm (1.35 +/- 0.22) and the control. In contrast, pCa(50) decreased slightly in Delta2Tm (5.11 +/- 0.07), and increased significantly in Delta3Tm (5.57 +/- 0.09) compared to the control (5.28 +/- 0.04). These results demonstrate that, when ions are present at physiological concentrations in the muscle fiber system, period 3 (but not period 2) is essential for the positive allosteric effect that enhances the interaction between actin and myosin, and increases isometric force of each cross-bridge.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2009 ","pages":"380967"},"PeriodicalIF":0.0,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2009/380967","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28694322","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-01-01Epub Date: 2010-02-09DOI: 10.1155/2009/819635
S Skrzyński, A Sionkowska, A Marciniak
Differential scanning calorimetry (DSC) has been used to estimate the effect of disc disease on the collagen helix-coil transition and morphology for tissue extracted from patients during surgical operation. Forty discs were obtained from patients with degenerative disc disease undergoing surgery for low back pain. The patients were in the age between 20 and 70 years old. The specimens were kept wet during DSC experiment. The data allow the comparison between thermal stability of collagen tissue from healthy patients and from patients suffering from disc disease. In the paper the comparison between thermal helix-coil transition for collagen fibers from patients suffering from disc disease and collagen fibers from healthy organisms has been discussed. The heating rate has an influence on the position on denaturation temperatures of collagen in disc tissues. Higher helix-coil transition temperature of collagen in degenerated disc suggests that additional intermolecular cross linking of collagen fibers occurs. Denaturation temperatures of collagen in degenerated male disc possess smaller values than in female ones. Disc disease induces changes in collagen structure and leads to formation of additional crosslinks between collagen fibers.
{"title":"DSC Study of Collagen in Disc Disease.","authors":"S Skrzyński, A Sionkowska, A Marciniak","doi":"10.1155/2009/819635","DOIUrl":"https://doi.org/10.1155/2009/819635","url":null,"abstract":"<p><p>Differential scanning calorimetry (DSC) has been used to estimate the effect of disc disease on the collagen helix-coil transition and morphology for tissue extracted from patients during surgical operation. Forty discs were obtained from patients with degenerative disc disease undergoing surgery for low back pain. The patients were in the age between 20 and 70 years old. The specimens were kept wet during DSC experiment. The data allow the comparison between thermal stability of collagen tissue from healthy patients and from patients suffering from disc disease. In the paper the comparison between thermal helix-coil transition for collagen fibers from patients suffering from disc disease and collagen fibers from healthy organisms has been discussed. The heating rate has an influence on the position on denaturation temperatures of collagen in disc tissues. Higher helix-coil transition temperature of collagen in degenerated disc suggests that additional intermolecular cross linking of collagen fibers occurs. Denaturation temperatures of collagen in degenerated male disc possess smaller values than in female ones. Disc disease induces changes in collagen structure and leads to formation of additional crosslinks between collagen fibers.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2009 ","pages":"819635"},"PeriodicalIF":0.0,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2009/819635","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28726048","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The crystal structure of a putative dipeptidase (Phdpd) from Pyrococcus horikoshii OT3 was solved using X-ray data at 2.4 A resolution. The protein is folded into two distinct entities. The N-terminal domain consists of the general topology of the alpha/beta fold, and the C-terminal domain consists of five long mixed strands, four helices, and two 3(10) helices. The structure of Phdpd is quite similar to reported structures of prolidases from P. furiosus (Zn-Pfprol) and P. horikoshii (Zn-Phdpd), where Zn ions are observed in the active site resulting in an inactive form. However, Phdpd did not contain metals in the crystal structure and showed prolidase activity in the absence of additional Co ions, whereas the specific activities increased by 5 times in the presence of a sufficient concentration (1.2 mM) of Co ions. The substrate specificities (X-Pro) of Phdpd were broad compared with those of Zn-Phdpd in the presence of Co ions, whose relative activities are 10% or less for substrates other than Met-Pro, which is the most favorable substrate. The binding constants of Zn-Phdpd with three metals (Zn, Co, and Mn) were higher than those of Phdpd and that with Zn was higher by greater than 2 orders, which were determined by DSC experiments. From the structural comparison of both forms and the above experimental results, it could be elucidated why the protein with Zn(2+) ions is inactive.
{"title":"Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3.","authors":"Jeyaraman Jeyakanthan, Katsumi Takada, Masahide Sawano, Kyoko Ogasahara, Hisashi Mizutani, Naoki Kunishima, Shigeyuki Yokoyama, Katsuhide Yutani","doi":"10.1155/2009/434038","DOIUrl":"https://doi.org/10.1155/2009/434038","url":null,"abstract":"<p><p>The crystal structure of a putative dipeptidase (Phdpd) from Pyrococcus horikoshii OT3 was solved using X-ray data at 2.4 A resolution. The protein is folded into two distinct entities. The N-terminal domain consists of the general topology of the alpha/beta fold, and the C-terminal domain consists of five long mixed strands, four helices, and two 3(10) helices. The structure of Phdpd is quite similar to reported structures of prolidases from P. furiosus (Zn-Pfprol) and P. horikoshii (Zn-Phdpd), where Zn ions are observed in the active site resulting in an inactive form. However, Phdpd did not contain metals in the crystal structure and showed prolidase activity in the absence of additional Co ions, whereas the specific activities increased by 5 times in the presence of a sufficient concentration (1.2 mM) of Co ions. The substrate specificities (X-Pro) of Phdpd were broad compared with those of Zn-Phdpd in the presence of Co ions, whose relative activities are 10% or less for substrates other than Met-Pro, which is the most favorable substrate. The binding constants of Zn-Phdpd with three metals (Zn, Co, and Mn) were higher than those of Phdpd and that with Zn was higher by greater than 2 orders, which were determined by DSC experiments. From the structural comparison of both forms and the above experimental results, it could be elucidated why the protein with Zn(2+) ions is inactive.</p>","PeriodicalId":73623,"journal":{"name":"Journal of biophysics (Hindawi Publishing Corporation : Online)","volume":"2009 ","pages":"434038"},"PeriodicalIF":0.0,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2009/434038","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28692659","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}