Literature DB >> 21428321

Organization and dynamics of membrane probes and proteins utilizing the red edge excitation shift.

Sourav Haldar1, Arunima Chaudhuri, Amitabha Chattopadhyay.   

Abstract

Dynamics of confined water has interesting implications in the organization and function of molecular assemblies such as membranes. A direct consequence of this type of organization is the restriction imposed on the mobility of the constituent structural units. Interestingly, this restriction (confinement) of mobility couples the motion of solvent (water) molecules with the slow moving molecules in the assembly. It is in this context that the red edge excitation shift (REES) represents a sensitive approach to monitor the environment and dynamics around a fluorophore in such organized assemblies. A shift in the wavelength of maximum fluorescence emission toward higher wavelengths, caused by a shift in the excitation wavelength toward the red edge of the absorption band, is termed REES. REES relies on slow solvent reorientation in the excited state of a fluorophore that can be used to monitor the environment and dynamics around a fluorophore in a host assembly. In this article, we focus on the application of REES to monitor organization and dynamics of membrane probes and proteins.
© 2011 American Chemical Society

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Year:  2011        PMID: 21428321     DOI: 10.1021/jp200255e

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN: 1520-5207            Impact factor:   2.991


  19 in total

1.  Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.

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Journal:  J Fluoresc       Date:  2015-04-03       Impact factor: 2.217

2.  Aggregation Behavior of pHLIP in Aqueous Solution at Low Concentrations: A Fluorescence Study.

Authors:  Bhagyashree D Rao; Hirak Chakraborty; Sandro Keller; Amitabha Chattopadhyay
Journal:  J Fluoresc       Date:  2018-06-29       Impact factor: 2.217

3.  GFP fluorescence: A few lesser-known nuggets that make it work.

Authors:  Parijat Sarkar; Amitabha Chattopadhyay
Journal:  J Biosci       Date:  2018-07       Impact factor: 1.826

4.  Silicon-doped carbon quantum dots with blue and green emission are a viable ratiometric fluorescent probe for hydroquinone.

Authors:  Yingnan Liu; Yuanyuan Cao; Tong Bu; Xinyu Sun; Taotao Zhe; Chen Huang; Siyu Yao; Li Wang
Journal:  Mikrochim Acta       Date:  2019-06-10       Impact factor: 5.833

5.  Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.

Authors:  Sourav Haldar; Arunima Chaudhuri; Hong Gu; Roger E Koeppe; Mamata Kombrabail; G Krishnamoorthy; Amitabha Chattopadhyay
Journal:  J Phys Chem B       Date:  2012-08-30       Impact factor: 2.991

6.  Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.

Authors:  Hirak Chakraborty; Amitabha Chattopadhyay
Journal:  J Fluoresc       Date:  2017-07-07       Impact factor: 2.217

7.  Organization and dynamics of the N-terminal domain of chemokine receptor CXCR1 in reverse micelles: effect of graded hydration.

Authors:  Arunima Chaudhuri; Pritam Basu; Sourav Haldar; Mamata Kombrabail; G Krishnamoorthy; Krishna Rajarathnam; Amitabha Chattopadhyay
Journal:  J Phys Chem B       Date:  2013-01-28       Impact factor: 2.991

Review 8.  Dynamics of water and ions around DNA: What is so special about them?

Authors:  Him Shweta; Sobhan Sen
Journal:  J Biosci       Date:  2018-07       Impact factor: 1.826

9.  Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.

Authors:  Arunima Chaudhuri; Sourav Haldar; Haiyan Sun; Roger E Koeppe; Amitabha Chattopadhyay
Journal:  Biochim Biophys Acta       Date:  2013-10-19

10.  Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.

Authors:  Sreetama Pal; Roger E Koeppe; Amitabha Chattopadhyay
Journal:  J Fluoresc       Date:  2018-09-17       Impact factor: 2.217

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