The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by 51 V-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and a kd of 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC50 of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased e-ATP exchange rate (k = 6.5 × 10 �3 and 4.47 × 10 �3 s �1 for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.
{"title":"A Comparison between Vanadyl, Vanadate, and Decavanadate Effects in Actin Structure and Function: Combination of Several Spectroscopic Studies","authors":"S. Ramos, J. Moura, M. Aureliano","doi":"10.1155/2012/532904","DOIUrl":"https://doi.org/10.1155/2012/532904","url":null,"abstract":"The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by 51 V-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and a kd of 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC50 of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased e-ATP exchange rate (k = 6.5 × 10 �3 and 4.47 × 10 �3 s �1 for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"31 1","pages":"355-359"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86719129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Drop-coating deposition Raman (DCDR) spectroscopy was employed to study liposome suspensions. The method is based on a specific drying process on the hydrophobic surface that efficiently accumulates the macromolecular sample in a ring of the edge of the dried drop. We studied liposome suspensions purchased from two sources (Avanti Polar Lipids, Inc. and Sigma-Aldrich, Co.) and prepared under different conditions. Structure of the dried drop substantially depends on the lipid concentration, lipid composition of the sample, and used solvent. Optimal lipid concentration is about 0.3 mg/ml in all cases, asolectin and DSPC suspensions form compact dried drops when dissolved in water and phosphate buffer, respectively. Drying process of the sample drop does not influence the initial phase state (gel or liquid-crystalline) of the studied liposomes excepting DSPC from Sigma-Aldrich, Co.
{"title":"DCDR Spectroscopy as Efficient Tool for Liposome Studies: Aspect of Preparation Procedure Parameters","authors":"E. Kočišová, A. Vodáková, M. Procházka","doi":"10.1155/2012/182720","DOIUrl":"https://doi.org/10.1155/2012/182720","url":null,"abstract":"Drop-coating deposition Raman (DCDR) spectroscopy was employed to study liposome suspensions. The method is based on a specific drying process on the hydrophobic surface that efficiently accumulates the macromolecular sample in a ring of the edge of the dried drop. We studied liposome suspensions purchased from two sources (Avanti Polar Lipids, Inc. and Sigma-Aldrich, Co.) and prepared under different conditions. Structure of the dried drop substantially depends on the lipid concentration, lipid composition of the sample, and used solvent. Optimal lipid concentration is about 0.3 mg/ml in all cases, asolectin and DSPC suspensions form compact dried drops when dissolved in water and phosphate buffer, respectively. Drying process of the sample drop does not influence the initial phase state (gel or liquid-crystalline) of the studied liposomes excepting DSPC from Sigma-Aldrich, Co.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"20 1","pages":"349-353"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72759194","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Folding dynamics for β-structure loss and disordered structure gain were studied in a model β-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamic β-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of the β-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lower 𝑘𝑓, with less change of the unfolding rate, 𝑘𝑢, assuming two state behavior at higher temperatures.
{"title":"Impact of β-Turn Sequence on β-Hairpin Dynamics Studied with Infrared-Detected Temperature Jump","authors":"Alexander Popp, Ling Wu, T. Keiderling, K. Hauser","doi":"10.1155/2012/102423","DOIUrl":"https://doi.org/10.1155/2012/102423","url":null,"abstract":"Folding dynamics for β-structure loss and disordered structure gain were studied in a model β-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamic β-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of the β-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lower 𝑘𝑓, with less change of the unfolding rate, 𝑘𝑢, assuming two state behavior at higher temperatures.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"79 1","pages":"557-564"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83195085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Barbora Řezáčová, Y. Coïc, C. Zentz, P. Turpin, J. Štěpánek
We have introduced a new promising approach for the determination of pKa constants of oligopeptide intrinsic fluorophores and spectral components referring to their differently charged states. The method is based on the factor analysis of multiwavelength spectroscopic pH titration data. As an illustration, we present its application on the study of short segments of the MADS box, which is a highly conserved sequence of a so-called family of transcription factors, by techniques of UV absorption and fluorescence spectroscopies. Investigated oligopeptides contain no tryptophan but one tyrosine serving as an intrinsic fluorophore and absorber. The results indicate both good sensitivity and spectroscopic selectivity of our method, which thus may be considered as a complementary technique to conventional electrochemical methods.
{"title":"Spectroscopic Determination of pKa Constants of MADS Box Segments","authors":"Barbora Řezáčová, Y. Coïc, C. Zentz, P. Turpin, J. Štěpánek","doi":"10.1155/2012/674032","DOIUrl":"https://doi.org/10.1155/2012/674032","url":null,"abstract":"We have introduced a new promising approach for the determination of pKa constants of oligopeptide intrinsic fluorophores and spectral components referring to their differently charged states. The method is based on the factor analysis of multiwavelength spectroscopic pH titration data. As an illustration, we present its application on the study of short segments of the MADS box, which is a highly conserved sequence of a so-called family of transcription factors, by techniques of UV absorption and fluorescence spectroscopies. Investigated oligopeptides contain no tryptophan but one tyrosine serving as an intrinsic fluorophore and absorber. The results indicate both good sensitivity and spectroscopic selectivity of our method, which thus may be considered as a complementary technique to conventional electrochemical methods.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"6 1","pages":"455-461"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91316090","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M. Polakovs, Ņ. Mironova-Ulmane, A. Pavlenko, E. Reinholds, M. Gavare, M. Grube, P. Stradins
In the present work we report results of investigations of human blood before and after radioisotope Tc 99m diagnosis by electron paramagnetic resonance (EPR) and Fourier transform infrared (FTIR) spectroscopies. It is shown that EPR can detect the concentration of methaemoglobin and transferrin ions more accurately than any other technique. FTIR spectra indicated that radiation caused conformational and concentration changes of proteins. Hierarchical cluster analysis (HCA) was created as time-saving tool for discrimination of initial and irradiated in vivo human blood samples.
{"title":"EPR and FTIR Spectroscopies Study of Human Blood after Irradiation","authors":"M. Polakovs, Ņ. Mironova-Ulmane, A. Pavlenko, E. Reinholds, M. Gavare, M. Grube, P. Stradins","doi":"10.1155/2012/365056","DOIUrl":"https://doi.org/10.1155/2012/365056","url":null,"abstract":"In the present work we report results of investigations of human blood before and after radioisotope Tc 99m diagnosis by electron paramagnetic resonance (EPR) and Fourier transform infrared (FTIR) spectroscopies. It is shown that EPR can detect the concentration of methaemoglobin and transferrin ions more accurately than any other technique. FTIR spectra indicated that radiation caused conformational and concentration changes of proteins. Hierarchical cluster analysis (HCA) was created as time-saving tool for discrimination of initial and irradiated in vivo human blood samples.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"57 1","pages":"367-371"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84416095","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Catarina S. H. Jesus, Daniela C. Vaz, M. Saraiva, R. Brito
Transthyretin (TTR) is a homotetrameric protein implicated in several amyloid diseases. The mechanism by which TTR is converted into elongated fibrillar assemblies has been extensively investigated, and numerous studies showed that dissociation of the native tetrameric structure into partially unfolded monomeric species precedes amyloid formation. The small differences observed in the crystal structures of different TTR variants, as well as the thermodynamics and kinetics of tetramer dissociation, do not seem to completely justify the amyloidogenic potential of different TTR variants. With this in mind, we have studied the refolding kinetics of WT-TTR and its most common amyloidogenic variant V30M-TTR, monitoring changes in intrinsic tryptophan fluorescence at different urea and protein concentrations. Our results demonstrate that the in vitro refolding mechanisms of WT- and V30M-TTR are similar, involving a dimeric intermediate. However, there are large differences in the refolding rate constants for the two variants, specially close to physiological conditions. Interestingly, tetramer formation occurs at a much slower rate in the amyloidogenic variant V30M-TTR than in WT-TTR, which in the in vivo setting may promote the accumulation of monomeric species in the extracellular environment, resulting in higher susceptibility for aggregation and amyloid formation instead of spontaneous refolding.
{"title":"The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin","authors":"Catarina S. H. Jesus, Daniela C. Vaz, M. Saraiva, R. Brito","doi":"10.1155/2012/502497","DOIUrl":"https://doi.org/10.1155/2012/502497","url":null,"abstract":"Transthyretin (TTR) is a homotetrameric protein implicated in several amyloid diseases. The mechanism by which TTR is converted into elongated fibrillar assemblies has been extensively investigated, and numerous studies showed that dissociation of the native tetrameric structure into partially unfolded monomeric species precedes amyloid formation. The small differences observed in the crystal structures of different TTR variants, as well as the thermodynamics and kinetics of tetramer dissociation, do not seem to completely justify the amyloidogenic potential of different TTR variants. With this in mind, we have studied the refolding kinetics of WT-TTR and its most common amyloidogenic variant V30M-TTR, monitoring changes in intrinsic tryptophan fluorescence at different urea and protein concentrations. Our results demonstrate that the in vitro refolding mechanisms of WT- and V30M-TTR are similar, involving a dimeric intermediate. However, there are large differences in the refolding rate constants for the two variants, specially close to physiological conditions. Interestingly, tetramer formation occurs at a much slower rate in the amyloidogenic variant V30M-TTR than in WT-TTR, which in the in vivo setting may promote the accumulation of monomeric species in the extracellular environment, resulting in higher susceptibility for aggregation and amyloid formation instead of spontaneous refolding.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"32 1","pages":"343-348"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81248114","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ana L. M. Batista de Carvalho, S. M. Fiuza, J. Tomkinson, Luís A. E. Batista de Carvalho, M. Paula M. Marques
A conformational analysis of the Pt(dap)Cl2 complex (dap=1,3-diaminopropane) was performed by vibrational spectroscopy (FTIR, Raman, and INS), coupled to quantum mechanical methods within the density functional theory (DFT) and effective core potential (ECP) approaches. A complete spectral assignment of the system was achieved, due to the combined use of all available vibrational spectroscopic techniques. A good agreement was found between experimental and theoretical results, as well as with reported data for analogous complexes (e.g., cisplatin).
{"title":"Pt(II) Complexes with Linear Diamines—Part I: Vibrational Study of Pt-Diaminopropane","authors":"Ana L. M. Batista de Carvalho, S. M. Fiuza, J. Tomkinson, Luís A. E. Batista de Carvalho, M. Paula M. Marques","doi":"10.1155/2012/206297","DOIUrl":"https://doi.org/10.1155/2012/206297","url":null,"abstract":"A conformational analysis of the Pt(dap)Cl2 complex (dap=1,3-diaminopropane) was performed by vibrational spectroscopy (FTIR, Raman, and INS), coupled to quantum mechanical methods within the density functional theory (DFT) and effective core potential (ECP) approaches. A complete spectral assignment of the system was achieved, due to the combined use of all available vibrational spectroscopic techniques. A good agreement was found between experimental and theoretical results, as well as with reported data for analogous complexes (e.g., cisplatin).","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"211 1","pages":"403-413"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77753284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
G. Graça, Sílvia O. Diaz, J. Pinto, António S. Barros, I. Duarte, B. Goodfellow, E. Galhano, Cristina Pita, Maria do Céu Almeida, I. Carreira, Ana M. Gil
This paper describes a metabonomics study of 2nd trimester biofluids (amniotic fluid, maternal urine, and blood plasma), in an attempt to correlate biofluid metabolic changes with suspected/diagnosed fetal malformations (FM) and chromosomal disorders as well as with later occurring gestational diabetes mellitus (GDM), preterm delivery (PTD), and premature rupture of membranes (PROM). The global biochemical picture given by the threesome of biofluids should enable the definition of potential disease signatures and unveil potential metabolite markers for clinical use in predictive prenatal diagnostics. Results show that relatively strong metabolic disturbances accompany FM, reflected in all three biofluids and thus suggesting the involvement of both fetal and maternal metabolisms. Regarding GDM, amniotic fluid and maternal urine seem potential good media to detect early metabolic changes, and PTD subjects show small metabolite changes in the same biofluids, undergoing work being focused on plasma composition. Chromosomal disorders show an interestingly marked effect on maternal urine, whereas no statistically relevant early changes have been observed for PROM subjects. Interestingly, in the case of FM and chromosomal disorders, maternal biofluids show some sensitivity to disorder type, for example, for central nervous system malformations and trisomy 21, respectively. These results show the usefulness of biofluid metabonomics to probe overall metabolic disturbances in relation to prenatal disorders.
{"title":"Can Biofluids Metabolic Profiling Help to Improve Healthcare during Pregnancy","authors":"G. Graça, Sílvia O. Diaz, J. Pinto, António S. Barros, I. Duarte, B. Goodfellow, E. Galhano, Cristina Pita, Maria do Céu Almeida, I. Carreira, Ana M. Gil","doi":"10.1155/2012/128367","DOIUrl":"https://doi.org/10.1155/2012/128367","url":null,"abstract":"This paper describes a metabonomics study of 2nd trimester biofluids (amniotic fluid, maternal urine, and blood plasma), in an attempt to correlate biofluid metabolic changes with suspected/diagnosed fetal malformations (FM) and chromosomal disorders as well as with later occurring gestational diabetes mellitus (GDM), preterm delivery (PTD), and premature rupture of membranes (PROM). The global biochemical picture given by the threesome of biofluids should enable the definition of potential disease signatures and unveil potential metabolite markers for clinical use in predictive prenatal diagnostics. Results show that relatively strong metabolic disturbances accompany FM, reflected in all three biofluids and thus suggesting the involvement of both fetal and maternal metabolisms. Regarding GDM, amniotic fluid and maternal urine seem potential good media to detect early metabolic changes, and PTD subjects show small metabolite changes in the same biofluids, undergoing work being focused on plasma composition. Chromosomal disorders show an interestingly marked effect on maternal urine, whereas no statistically relevant early changes have been observed for PROM subjects. Interestingly, in the case of FM and chromosomal disorders, maternal biofluids show some sensitivity to disorder type, for example, for central nervous system malformations and trisomy 21, respectively. These results show the usefulness of biofluid metabonomics to probe overall metabolic disturbances in relation to prenatal disorders.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"21 1","pages":"515-523"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76518479","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
E. Chikhirzhina, T. Starkova, Elena Kostyleva, A. Polyanichko
The interaction of the linker histone H1Z from the sperm chromatin of starfish Asterias amurensis with DNA was studied by spectroscopic and thermodynamic approaches. It has been shown that at the physiological conditions the interaction of the H1Z with DNA results in more compact structures compared to complexes of DNA with somatic histone H1. The typical profile of the DNA melting curves reveals two peaks attributed to the bound and unbound DNA. It has been shown that H1Z from starfish sperm stabilizes DNA to a greater extent compared to the somatic H1. It is possible that the presence of the additional α—helical segments within the C-terminal part of the H1Z typical for the linker histones from echinoderm sperm facilitates the protein-protein interactions which in turn stimulate cooperative binding of the histones to DNA, resulting in the formation of the supercompact sperm chromatin.
{"title":"Spectroscopic Study of the Interaction of DNA with the Linker Histone H1 from Starfish Sperm Reveals Mechanisms of the Formation of Supercondensed Sperm Chromatin","authors":"E. Chikhirzhina, T. Starkova, Elena Kostyleva, A. Polyanichko","doi":"10.1155/2012/250489","DOIUrl":"https://doi.org/10.1155/2012/250489","url":null,"abstract":"The interaction of the linker histone H1Z from the sperm chromatin of starfish Asterias amurensis with DNA was studied by spectroscopic and thermodynamic approaches. It has been shown that at the physiological conditions the interaction of the H1Z with DNA results in more compact structures compared to complexes of DNA with somatic histone H1. The typical profile of the DNA melting curves reveals two peaks attributed to the bound and unbound DNA. It has been shown that H1Z from starfish sperm stabilizes DNA to a greater extent compared to the somatic H1. It is possible that the presence of the additional α—helical segments within the C-terminal part of the H1Z typical for the linker histones from echinoderm sperm facilitates the protein-protein interactions which in turn stimulate cooperative binding of the histones to DNA, resulting in the formation of the supercompact sperm chromatin.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"44 1","pages":"433-440"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80276179","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rapid and reproducible discrimination between bacterial pathogens is a clear goal in microbiological laboratories when processing infected clinical samples. In this study Raman spectra were taken from at least 30 colonies of four strains of bacteria including Staphylococcus epidermidis (1457 and 9142) and Escherichia coli (K12 and Top 10) using the Renishaw in Via Raman microscope system. Analysis based on principal components suggests that even strain differentiation (e.g., 1457 versus 9142 or K12 versus Top10) is possible.
在处理感染的临床样本时，微生物实验室的一个明确目标是快速和可重复地区分细菌病原体。本研究利用Renishaw In Via拉曼显微镜系统采集了4株表皮葡萄球菌(1457和9142)和大肠杆菌(K12和Top 10)至少30个菌落的拉曼光谱。基于主成分的分析表明，即使应变分化(例如，1457与9142或K12与Top10)也是可能的。
{"title":"Raman Spectroscopy of Bacterial Species and Strains Cultivated under Reproducible Conditions","authors":"J. Almarashi, N. Kapel, T. S. Wilkinson, H. Telle","doi":"10.1155/2012/540490","DOIUrl":"https://doi.org/10.1155/2012/540490","url":null,"abstract":"Rapid and reproducible discrimination between bacterial pathogens is a clear goal in microbiological laboratories when processing infected clinical samples. In this study Raman spectra were taken from at least 30 colonies of four strains of bacteria including Staphylococcus epidermidis (1457 and 9142) and Escherichia coli (K12 and Top 10) using the Renishaw in Via Raman microscope system. Analysis based on principal components suggests that even strain differentiation (e.g., 1457 versus 9142 or K12 versus Top10) is possible.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"33 1","pages":"361-365"},"PeriodicalIF":0.0,"publicationDate":"2012-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79397528","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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