We propose an improved prediction method of the tertiary structures of $alpha$-helical membrane proteins based on the replica-exchange method by taking into account helix deformations. Our method allows wide applications because transmembrane helices of native membrane proteins are often distorted. In order to test the effectiveness of the present method, we applied it to the structure predictions of glycophorin A and phospholamban. The results were in accord with experiments.
{"title":"Predictions of tertiary stuctures of $alpha$-helical membrane proteins by replica-exchange method with consideration of helix deformations","authors":"Ryo Urano, H. Kokubo, Y. Okamoto","doi":"10.7566/JPSJ.84.084802","DOIUrl":"https://doi.org/10.7566/JPSJ.84.084802","url":null,"abstract":"We propose an improved prediction method of the tertiary structures of $alpha$-helical membrane proteins based on the replica-exchange method by taking into account helix deformations. Our method allows wide applications because transmembrane helices of native membrane proteins are often distorted. In order to test the effectiveness of the present method, we applied it to the structure predictions of glycophorin A and phospholamban. The results were in accord with experiments.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84960861","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}
The need of new diagnostic methods satisfying, as an early detection, a low invasive procedure and a cost-efficient value, is orienting the technological research toward the use of bio-integrated devices, in particular bio-sensors. The set of know-why necessary to achieve this goal is wide, from biochemistry to electronics and is summarized in an emerging branch of electronics, called textit{proteotronics}. Proteotronics is here here applied to state a comparative analysis of the electrical responses coming from type-1 and type-2 opsins. In particular, the procedure is used as an early investigation of a recently discovered family of opsins, the proteorhodopsins activated by blue light, BPRs. The results reveal some interesting and unexpected similarities between proteins of the two families, suggesting the global electrical response are not strictly linked to the class identity.
{"title":"Opsin vs opsin: new materials for biotechnological applications","authors":"E. Alfinito, L. Reggiani","doi":"10.1063/1.4892445","DOIUrl":"https://doi.org/10.1063/1.4892445","url":null,"abstract":"The need of new diagnostic methods satisfying, as an early detection, a low invasive procedure and a cost-efficient value, is orienting the technological research toward the use of bio-integrated devices, in particular bio-sensors. The set of know-why necessary to achieve this goal is wide, from biochemistry to electronics and is summarized in an emerging branch of electronics, called textit{proteotronics}. Proteotronics is here here applied to state a comparative analysis of the electrical responses coming from type-1 and type-2 opsins. In particular, the procedure is used as an early investigation of a recently discovered family of opsins, the proteorhodopsins activated by blue light, BPRs. The results reveal some interesting and unexpected similarities between proteins of the two families, suggesting the global electrical response are not strictly linked to the class identity.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-02-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89160433","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}
Pub Date : 2014-01-30DOI: 10.7287/PEERJ.PREPRINTS.229V1
Penghui Shi
Zinc-finger nucleases (ZFNs) and transcription activator-like effector nucleases (TALENs) comprise a powerful class of tools that are redefining the boundaries of biological research. Although these technologies have begun to enable targeted genome modifications, there remains a need for new technologies that are scalable, affordable, and easy to engineer. In this paper, we propose a new tool for genetic engineering, the pseudocomplementary peptide nucleic acid nucleases (pcPNANs), which are composed of a pseudocomplementary PNA (pcPNA) specific for a DNA target sequence, a FokI nuclease cleavage domain and a nuclear localization signal. pcPNANs may induce targeted DNA double-strand breaks that activate DNA damage response pathways and enable custom alterations. Their cleavage-site is determined by simple Watson-Crick rule, and thus pcPNANs for aimed cleavage of genomes can be straightforwardly designed and synthesized without any selection procedure. Accordingly, the cleavage-site and site-specificity are freely chosen by changing the sequences and the lengths of pcPNA strands. We believe that the potentiality of pcPNAN as a new tool for genetic engineering will be confirmed in the future.
{"title":"Can pseudocomplementary peptide nucleic acid nucleases (pcPNANs) be a new tool for genetic engineering","authors":"Penghui Shi","doi":"10.7287/PEERJ.PREPRINTS.229V1","DOIUrl":"https://doi.org/10.7287/PEERJ.PREPRINTS.229V1","url":null,"abstract":"Zinc-finger nucleases (ZFNs) and transcription activator-like effector nucleases (TALENs) comprise a powerful class of tools that are redefining the boundaries of biological research. Although these technologies have begun to enable targeted genome modifications, there remains a need for new technologies that are scalable, affordable, and easy to engineer. In this paper, we propose a new tool for genetic engineering, the pseudocomplementary peptide nucleic acid nucleases (pcPNANs), which are composed of a pseudocomplementary PNA (pcPNA) specific for a DNA target sequence, a FokI nuclease cleavage domain and a nuclear localization signal. pcPNANs may induce targeted DNA double-strand breaks that activate DNA damage response pathways and enable custom alterations. Their cleavage-site is determined by simple Watson-Crick rule, and thus pcPNANs for aimed cleavage of genomes can be straightforwardly designed and synthesized without any selection procedure. Accordingly, the cleavage-site and site-specificity are freely chosen by changing the sequences and the lengths of pcPNA strands. We believe that the potentiality of pcPNAN as a new tool for genetic engineering will be confirmed in the future.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84545580","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}
O. O. Liubysh, O. Alekseev, S. Tkachov, S. Perepelytsya
The effects of ionic ordering in DNA water solutions are studied by conductivity experiments. The conductivity measurements are performed for the solutions of DNA with KCl salt in the temperature range from 28 to 70 C. Salt concentration vary from 0 to 2 M. The conductivity of solutions without DNA but with the same concentration of KCl salt are also performed. The results show that in case of salt free solution of DNA the melting process of the double helix is observed, while in case of DNA solution with added salt the macromolecule denaturation is not featured. For salt concentrations lower than some critical one (0.4 M) the conductivity of DNA solution is higher than the conductivity of KCl water solution without DNA. Starting from the critical concentration the conductivity of KCl solution is higher than the conductivity of DNA solution with added salt. For description of the experimental data phenomenological model is elaborated basing on electrolyte theory. In framework of the developed model a mechanism of counterion ordering is introduced. According to this mechanism under the low salt concentrations electrical conductivity of the system is caused by counterions of DNA ion-hydrate shell. Increasing the amount of salt to the critical concentration counterions condense on DNA polyanion. Further increase of salt concentration leads to the formation of DNA-salt complexes that decreases the conductivity of the system.
{"title":"Effect of ionic ordering in conductivity experiments of DNA aqueous solutions","authors":"O. O. Liubysh, O. Alekseev, S. Tkachov, S. Perepelytsya","doi":"10.15407/UJPE59.05.0479","DOIUrl":"https://doi.org/10.15407/UJPE59.05.0479","url":null,"abstract":"The effects of ionic ordering in DNA water solutions are studied by conductivity experiments. The conductivity measurements are performed for the solutions of DNA with KCl salt in the temperature range from 28 to 70 C. Salt concentration vary from 0 to 2 M. The conductivity of solutions without DNA but with the same concentration of KCl salt are also performed. The results show that in case of salt free solution of DNA the melting process of the double helix is observed, while in case of DNA solution with added salt the macromolecule denaturation is not featured. For salt concentrations lower than some critical one (0.4 M) the conductivity of DNA solution is higher than the conductivity of KCl water solution without DNA. Starting from the critical concentration the conductivity of KCl solution is higher than the conductivity of DNA solution with added salt. For description of the experimental data phenomenological model is elaborated basing on electrolyte theory. In framework of the developed model a mechanism of counterion ordering is introduced. According to this mechanism under the low salt concentrations electrical conductivity of the system is caused by counterions of DNA ion-hydrate shell. Increasing the amount of salt to the critical concentration counterions condense on DNA polyanion. Further increase of salt concentration leads to the formation of DNA-salt complexes that decreases the conductivity of the system.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82579657","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}
A simple way to get insights about the possible functional motions of a protein is to perform a normal mode analysis (NMA). Indeed, it has been shown that low-frequency modes thus obtained are often closely related to domain motions involved in protein function. Moreover, because protein low-frequency modes are known to be robust, NMA can be performed using coarse-grained models. As a consequence, it can be done for large ensembles of conformations as well as for large systems, like the ribosome, whole virus capsids, etc. Unexpectedly, on the high-frequency side, modes obtained with cutoff-based coarse-grained models also seem able to provide useful insights on protein dynamical properties.
{"title":"Simplified flexibility analysis of proteins","authors":"Y. Sanejouand","doi":"10.1201/b17979-12","DOIUrl":"https://doi.org/10.1201/b17979-12","url":null,"abstract":"A simple way to get insights about the possible functional motions of a protein is to perform a normal mode analysis (NMA). Indeed, it has been shown that low-frequency modes thus obtained are often closely related to domain motions involved in protein function. Moreover, because protein low-frequency modes are known to be robust, NMA can be performed using coarse-grained models. As a consequence, it can be done for large ensembles of conformations as well as for large systems, like the ribosome, whole virus capsids, etc. Unexpectedly, on the high-frequency side, modes obtained with cutoff-based coarse-grained models also seem able to provide useful insights on protein dynamical properties.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88210671","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}
Pub Date : 2013-10-21DOI: 10.1103/PhysRevX.4.021002
Jaeoh Shin, Andrey G. Cherstvy, R. Metzler
The rapid worldwide spread of severe viral infections, often involving novel modifications of viruses, poses major challenges to our health care systems. This means that tools that can efficiently and specifically diagnose viruses are much needed. To be relevant for a broad application in local health care centers, such tools should be relatively cheap and easy to use. Here we discuss the biophysical potential for the macroscopic detection of viruses based on the induction of a mechanical stress in a bundle of pre-stretched DNA molecules upon binding of viruses to the DNA. We show that the affinity of the DNA to the charged virus surface induces a local melting of the double-helix into two single-stranded DNA. This process effects a mechanical stress along the DNA chains leading to an overall contraction of the DNA. Our results suggest that when such DNA bundles are incorporated in a supporting matrix such as a responsive hydrogel, the presence of viruses may indeed lead to a significant, macroscopic mechanical deformation of the matrix. We discuss the biophysical basis for this effect and characterize the physical properties of the associated DNA melting transition. In particular, we reveal several scaling relations between the relevant physical parameters of the system. We promote this DNA-based assay for efficient and specific virus screening.
{"title":"Sensing viruses by mechanical tension of DNA in responsive hydrogels","authors":"Jaeoh Shin, Andrey G. Cherstvy, R. Metzler","doi":"10.1103/PhysRevX.4.021002","DOIUrl":"https://doi.org/10.1103/PhysRevX.4.021002","url":null,"abstract":"The rapid worldwide spread of severe viral infections, often involving novel modifications of viruses, poses major challenges to our health care systems. This means that tools that can efficiently and specifically diagnose viruses are much needed. To be relevant for a broad application in local health care centers, such tools should be relatively cheap and easy to use. Here we discuss the biophysical potential for the macroscopic detection of viruses based on the induction of a mechanical stress in a bundle of pre-stretched DNA molecules upon binding of viruses to the DNA. We show that the affinity of the DNA to the charged virus surface induces a local melting of the double-helix into two single-stranded DNA. This process effects a mechanical stress along the DNA chains leading to an overall contraction of the DNA. Our results suggest that when such DNA bundles are incorporated in a supporting matrix such as a responsive hydrogel, the presence of viruses may indeed lead to a significant, macroscopic mechanical deformation of the matrix. We discuss the biophysical basis for this effect and characterize the physical properties of the associated DNA melting transition. In particular, we reveal several scaling relations between the relevant physical parameters of the system. We promote this DNA-based assay for efficient and specific virus screening.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75284580","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}
In the present study, the origin of the anti-quorum sensing (QS) activities of several members of a recently synthesized and in vitro tested class of lactone and thiolactone based inhibitors were computationally investigated. Docking and molecular dynamic (MD) simulations and binding free energy calculations were carried out to reveal the exact binding and inhibitory profiles of these compounds. The higher in vitro activity of the lactone series relative to their thiolactone isosteres was verified based on estimating the binding energies, the docking scores and monitoring the stability of the complexes produced in the MD simulations. The strong electrostatic contribution to the binding energies may be responsible for the higher inhibitory activity of the lactone with respect to the thiolactone series. The results of this study help to understand the anti-QS properties of lactone-based inhibitors and provide important information that may assist in the synthesis of novel QS inhibitors.
{"title":"In silico investigation of lactone and thiolactone inhibitors in bacterial quorum sensing using molecular modeling","authors":"Marawan Ahmed, S. Bird, Feng Wang, E. Palombo","doi":"10.5539/IJC.V5N4P9","DOIUrl":"https://doi.org/10.5539/IJC.V5N4P9","url":null,"abstract":"In the present study, the origin of the anti-quorum sensing (QS) activities of several members of a recently synthesized and in vitro tested class of lactone and thiolactone based inhibitors were computationally investigated. Docking and molecular dynamic (MD) simulations and binding free energy calculations were carried out to reveal the exact binding and inhibitory profiles of these compounds. The higher in vitro activity of the lactone series relative to their thiolactone isosteres was verified based on estimating the binding energies, the docking scores and monitoring the stability of the complexes produced in the MD simulations. The strong electrostatic contribution to the binding energies may be responsible for the higher inhibitory activity of the lactone with respect to the thiolactone series. The results of this study help to understand the anti-QS properties of lactone-based inhibitors and provide important information that may assist in the synthesis of novel QS inhibitors.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82969941","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}
The conformational vibrations of Z-DNA with counterions are studied in framework of phenomenological model developed. The structure of left-handed double helix with counterions neutralizing the negatively charged phosphate groups of DNA is considered as the ion-phosphate lattice. The frequencies and Raman intensities for the modes of Z-DNA with Na+ and Mg2+ ions are calculated, and the low-frequency Raman spectra are built. At the spectra range about the frequency 150 cm-1 new mode of ion-phosphate vibrations is found, which characterizes the vibrations of Mg2+ counterions. The results of our calculations show that the intensities of Z-DNA modes are sensitive to the concentration of magnesium counterions. The obtained results describe well the experimental Raman spectra of Z-DNA.
{"title":"Dynamics of ion-phosphate lattice of DNA in left-handed double helix form","authors":"S. Perepelytsya, S. Volkov","doi":"10.15407/UJPE58.06.0554","DOIUrl":"https://doi.org/10.15407/UJPE58.06.0554","url":null,"abstract":"The conformational vibrations of Z-DNA with counterions are studied in framework of phenomenological model developed. The structure of left-handed double helix with counterions neutralizing the negatively charged phosphate groups of DNA is considered as the ion-phosphate lattice. The frequencies and Raman intensities for the modes of Z-DNA with Na+ and Mg2+ ions are calculated, and the low-frequency Raman spectra are built. At the spectra range about the frequency 150 cm-1 new mode of ion-phosphate vibrations is found, which characterizes the vibrations of Mg2+ counterions. The results of our calculations show that the intensities of Z-DNA modes are sensitive to the concentration of magnesium counterions. The obtained results describe well the experimental Raman spectra of Z-DNA.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78833101","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}
Pub Date : 2013-02-08DOI: 10.1142/9789814449144_0011
Anil Korkut, W. Hendrickson
The conformations available to polypeptides are determined by the interatomic forces acting on the peptide units, whereby backbone torsion angles are restricted as described by the Ramachandran plot. Although typical proteins are composed predominantly from {alpha}-helices and {beta}-sheets, they nevertheless adopt diverse tertiary structure, each folded as dictated by its unique amino-acid sequence. Despite such uniqueness, however, the functioning of many proteins involves changes between quite different conformations. The study of large-scale conformational changes, particularly in large systems, is facilitated by a coarse-grained representation such as provided by virtually bonded C{alpha} atoms. We have developed a virtual atom molecular mechanics (VAMM) force field to describe conformational dynamics in proteins and a VAMM-based algorithm for computing conformational transition pathways. Here we describe the stereochemical analysis of proteins in this coarse-grained representation, comparing the relevant plots in coarse-grained conformational space to the corresponding Ramachandran plots, having contoured each at levels determined statistically from residues in a large database. The distributions shown for an all-{alpha} protein, two all-{beta} proteins and one {alpha}+{beta} protein serve to relate the coarse-grained distributions to the familiar Ramachandran plot.
{"title":"Stereochemistry of polypeptide conformation in coarse grained analysis","authors":"Anil Korkut, W. Hendrickson","doi":"10.1142/9789814449144_0011","DOIUrl":"https://doi.org/10.1142/9789814449144_0011","url":null,"abstract":"The conformations available to polypeptides are determined by the interatomic forces acting on the peptide units, whereby backbone torsion angles are restricted as described by the Ramachandran plot. Although typical proteins are composed predominantly from {alpha}-helices and {beta}-sheets, they nevertheless adopt diverse tertiary structure, each folded as dictated by its unique amino-acid sequence. Despite such uniqueness, however, the functioning of many proteins involves changes between quite different conformations. The study of large-scale conformational changes, particularly in large systems, is facilitated by a coarse-grained representation such as provided by virtually bonded C{alpha} atoms. We have developed a virtual atom molecular mechanics (VAMM) force field to describe conformational dynamics in proteins and a VAMM-based algorithm for computing conformational transition pathways. Here we describe the stereochemical analysis of proteins in this coarse-grained representation, comparing the relevant plots in coarse-grained conformational space to the corresponding Ramachandran plots, having contoured each at levels determined statistically from residues in a large database. The distributions shown for an all-{alpha} protein, two all-{beta} proteins and one {alpha}+{beta} protein serve to relate the coarse-grained distributions to the familiar Ramachandran plot.","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80021268","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}
Pub Date : 2012-11-12DOI: 10.1007/978-3-319-00395-5_58
P. Gaspard
{"title":"Dynamical Aspects of Information in Copolymerization Processes","authors":"P. Gaspard","doi":"10.1007/978-3-319-00395-5_58","DOIUrl":"https://doi.org/10.1007/978-3-319-00395-5_58","url":null,"abstract":"","PeriodicalId":8447,"journal":{"name":"arXiv: Biomolecules","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2012-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86883862","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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