Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation
Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appe...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
dos Remedios, Cristobal G. [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1987 |
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| Schlagwörter: |
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| Anmerkung: |
© Chapman and Hall Ltd 1987 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Kluwer Academic Publishers, 1980, 8(1987), 2 vom: Apr., Seite 97-117 |
|---|---|
| Übergeordnetes Werk: |
volume:8 ; year:1987 ; number:2 ; month:04 ; pages:97-117 |
| Links: |
|---|
| DOI / URN: |
10.1007/BF01753986 |
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OLC2067114565 |
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| 245 | 1 | 0 | |a Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation |
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| 520 | |a Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. | ||
| 650 | 4 | |a Crucial Role | |
| 650 | 4 | |a Energy Transfer | |
| 650 | 4 | |a Critical Evaluation | |
| 650 | 4 | |a Muscle Contraction | |
| 650 | 4 | |a Eukaryotic Cell | |
| 700 | 1 | |a Miki, Masao |4 aut | |
| 700 | 1 | |a Barden, Julian A. |4 aut | |
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10.1007/BF01753986 doi (DE-627)OLC2067114565 (DE-He213)BF01753986-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid dos Remedios, Cristobal G. verfasserin aut Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation 1987 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall Ltd 1987 Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. Crucial Role Energy Transfer Critical Evaluation Muscle Contraction Eukaryotic Cell Miki, Masao aut Barden, Julian A. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 8(1987), 2 vom: Apr., Seite 97-117 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:8 year:1987 number:2 month:04 pages:97-117 https://doi.org/10.1007/BF01753986 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 8 1987 2 04 97-117 |
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10.1007/BF01753986 doi (DE-627)OLC2067114565 (DE-He213)BF01753986-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid dos Remedios, Cristobal G. verfasserin aut Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation 1987 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall Ltd 1987 Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. Crucial Role Energy Transfer Critical Evaluation Muscle Contraction Eukaryotic Cell Miki, Masao aut Barden, Julian A. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 8(1987), 2 vom: Apr., Seite 97-117 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:8 year:1987 number:2 month:04 pages:97-117 https://doi.org/10.1007/BF01753986 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 8 1987 2 04 97-117 |
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10.1007/BF01753986 doi (DE-627)OLC2067114565 (DE-He213)BF01753986-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid dos Remedios, Cristobal G. verfasserin aut Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation 1987 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall Ltd 1987 Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. Crucial Role Energy Transfer Critical Evaluation Muscle Contraction Eukaryotic Cell Miki, Masao aut Barden, Julian A. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 8(1987), 2 vom: Apr., Seite 97-117 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:8 year:1987 number:2 month:04 pages:97-117 https://doi.org/10.1007/BF01753986 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 8 1987 2 04 97-117 |
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10.1007/BF01753986 doi (DE-627)OLC2067114565 (DE-He213)BF01753986-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid dos Remedios, Cristobal G. verfasserin aut Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation 1987 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall Ltd 1987 Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. Crucial Role Energy Transfer Critical Evaluation Muscle Contraction Eukaryotic Cell Miki, Masao aut Barden, Julian A. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 8(1987), 2 vom: Apr., Seite 97-117 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:8 year:1987 number:2 month:04 pages:97-117 https://doi.org/10.1007/BF01753986 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 8 1987 2 04 97-117 |
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10.1007/BF01753986 doi (DE-627)OLC2067114565 (DE-He213)BF01753986-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid dos Remedios, Cristobal G. verfasserin aut Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation 1987 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall Ltd 1987 Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. Crucial Role Energy Transfer Critical Evaluation Muscle Contraction Eukaryotic Cell Miki, Masao aut Barden, Julian A. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 8(1987), 2 vom: Apr., Seite 97-117 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:8 year:1987 number:2 month:04 pages:97-117 https://doi.org/10.1007/BF01753986 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 8 1987 2 04 97-117 |
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dos Remedios, Cristobal G. Miki, Masao Barden, Julian A. |
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dos Remedios, Cristobal G. |
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fluorescence resonance energy transfer measurements of distances in actin and myosin. a critical evaluation |
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Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation |
| abstract |
Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. © Chapman and Hall Ltd 1987 |
| abstractGer |
Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. © Chapman and Hall Ltd 1987 |
| abstract_unstemmed |
Summary The contractile proteins actin and myosin are of considerable biological interest. They are essential for muscle contraction and in eukaryotic cells they play a crucial role in most contractile phenomena. Over the years since the first fluorescence resonance energy transfer (FRET) paper appeared, an extensive body of literature has accumulated on this technique using actin, myosin and the actomyosin complex. These papers are reviewed with several aims in mind: (i) we assess the reliability and consistency of intra- and inter-molecular distances measured between the fluorescent probes attached to specific sites on these proteins; (ii) we determine whether the measurements can be assembled into an internally consistent model which can be fitted to the known dimensions of the actomyosin complex; (iii) several of the FRET distances are consistent with the available structural data from crystallographic and electron microscopic dimensions; (iv) the modelled FRET distances suggest that the assumed value of the orientation factor (K2 = 2/3) is reasonable; (v) we conclude that the model has a predictive value, i.e. it suggests that a small number of the published dimensions may be incorrect and predicts the magnitude of a larger number of measurements which have not yet been reported; and finally (vi) we discuss the contribution of FRET determinations to the current debate on the molecular mechanism of contraction. © Chapman and Hall Ltd 1987 |
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Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation |
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