Abstract
Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.
| Original language | English |
|---|---|
| Pages (from-to) | 861-876 |
| Number of pages | 16 |
| Journal | Biophysical Reviews |
| Volume | 9 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Dec 1 2017 |
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Keywords
- Energy conversion
- Membrane protein
- Retinal
- Rhodopsin
- Signal transduction
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology
Cite this
Conversion of microbial rhodopsins : insights into functionally essential elements and rational protein engineering. / Kaneko, Akimasa; Inoue, Keiichi; Kojima, Keiichi; Kandori, Hideki; Sudo, Yuki.
In: Biophysical Reviews, Vol. 9, No. 6, 01.12.2017, p. 861-876.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Conversion of microbial rhodopsins
T2 - insights into functionally essential elements and rational protein engineering
AU - Kaneko, Akimasa
AU - Inoue, Keiichi
AU - Kojima, Keiichi
AU - Kandori, Hideki
AU - Sudo, Yuki
PY - 2017/12/1
Y1 - 2017/12/1
N2 - Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.
AB - Technological progress has enabled the successful application of functional conversion to a variety of biological molecules, such as nucleotides and proteins. Such studies have revealed the functionally essential elements of these engineered molecules, which are difficult to characterize at the level of an individual molecule. The functional conversion of biological molecules has also provided a strategy for their rational and atomistic design. The engineered molecules can be used in studies to improve our understanding of their biological functions and to develop protein-based tools. In this review, we introduce the functional conversion of membrane-embedded photoreceptive retinylidene proteins (also called rhodopsins) and discuss these proteins mainly on the basis of results obtained from our own studies. This information provides insights into the molecular mechanism of light-induced protein functions and their use in optogenetics, a technology which involves the use of light to control biological activities.
KW - Energy conversion
KW - Membrane protein
KW - Retinal
KW - Rhodopsin
KW - Signal transduction
UR - http://www.scopus.com/inward/record.url?scp=85037133773&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85037133773&partnerID=8YFLogxK
U2 - 10.1007/s12551-017-0335-x
DO - 10.1007/s12551-017-0335-x
M3 - Review article
VL - 9
SP - 861
EP - 876
JO - Biophysical Reviews
JF - Biophysical Reviews
SN - 1867-2450
IS - 6
ER -