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Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein
In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a...
| Clasificación: | Libro Electrónico |
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| Autor principal: | |
| Autor Corporativo: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Cham :
Springer International Publishing : Imprint: Springer,
2016.
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| Edición: | 1st ed. 2016. |
| Colección: | Springer Theses, Recognizing Outstanding Ph.D. Research,
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| Temas: | |
| Acceso en línea: | Texto Completo |
MARC
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| 001 | 978-3-319-09558-5 | ||
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| 005 | 20220119081209.0 | ||
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| 008 | 151017s2016 sz | s |||| 0|eng d | ||
| 020 | |a 9783319095585 |9 978-3-319-09558-5 | ||
| 024 | 7 | |a 10.1007/978-3-319-09558-5 |2 doi | |
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| 100 | 1 | |a Cohen, Sharona. |e author. |4 aut |4 http://id.loc.gov/vocabulary/relators/aut | |
| 245 | 1 | 0 | |a Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein |h [electronic resource] / |c by Sharona Cohen. |
| 250 | |a 1st ed. 2016. | ||
| 264 | 1 | |a Cham : |b Springer International Publishing : |b Imprint: Springer, |c 2016. | |
| 300 | |a XIII, 59 p. 28 illus. in color. |b online resource. | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 347 | |a text file |b PDF |2 rda | ||
| 490 | 1 | |a Springer Theses, Recognizing Outstanding Ph.D. Research, |x 2190-5061 | |
| 505 | 0 | |a Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans. | |
| 520 | |a In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field. | ||
| 650 | 0 | |a Bioorganic chemistry. | |
| 650 | 0 | |a Spectrum analysis. | |
| 650 | 0 | |a Biophysics. | |
| 650 | 1 | 4 | |a Bioorganic Chemistry. |
| 650 | 2 | 4 | |a Spectroscopy. |
| 650 | 2 | 4 | |a Biophysics. |
| 710 | 2 | |a SpringerLink (Online service) | |
| 773 | 0 | |t Springer Nature eBook | |
| 776 | 0 | 8 | |i Printed edition: |z 9783319095578 |
| 776 | 0 | 8 | |i Printed edition: |z 9783319095592 |
| 776 | 0 | 8 | |i Printed edition: |z 9783319372365 |
| 830 | 0 | |a Springer Theses, Recognizing Outstanding Ph.D. Research, |x 2190-5061 | |
| 856 | 4 | 0 | |u https://doi.uam.elogim.com/10.1007/978-3-319-09558-5 |z Texto Completo |
| 912 | |a ZDB-2-CMS | ||
| 912 | |a ZDB-2-SXC | ||
| 950 | |a Chemistry and Materials Science (SpringerNature-11644) | ||
| 950 | |a Chemistry and Material Science (R0) (SpringerNature-43709) | ||