268 related articles for article (PubMed ID: 23981188)
1. Dynamic insight into protein structure utilizing red edge excitation shift.
Chattopadhyay A; Haldar S
Acc Chem Res; 2014 Jan; 47(1):12-9. PubMed ID: 23981188
[TBL] [Abstract][Full Text] [Related]
2. Organization and dynamics of membrane probes and proteins utilizing the red edge excitation shift.
Haldar S; Chaudhuri A; Chattopadhyay A
J Phys Chem B; 2011 May; 115(19):5693-706. PubMed ID: 21428321
[TBL] [Abstract][Full Text] [Related]
3. Organization and dynamics of tryptophans in the molten globule state of bovine alpha-lactalbumin utilizing wavelength-selective fluorescence approach: comparisons with native and denatured states.
Chaudhuri A; Haldar S; Chattopadhyay A
Biochem Biophys Res Commun; 2010 Apr; 394(4):1082-6. PubMed ID: 20346348
[TBL] [Abstract][Full Text] [Related]
4. Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach.
Chattopadhyay A
Chem Phys Lipids; 2003 Jan; 122(1-2):3-17. PubMed ID: 12598034
[TBL] [Abstract][Full Text] [Related]
5. Dipolar relaxation within the protein matrix of the green fluorescent protein: a red edge excitation shift study.
Haldar S; Chattopadhyay A
J Phys Chem B; 2007 Dec; 111(51):14436-9. PubMed ID: 18052368
[TBL] [Abstract][Full Text] [Related]
6. Organization and dynamics of tryptophan residues in erythroid spectrin: novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach.
Chattopadhyay A; Rawat SS; Kelkar DA; Ray S; Chakrabarti A
Protein Sci; 2003 Nov; 12(11):2389-403. PubMed ID: 14573853
[TBL] [Abstract][Full Text] [Related]
7. Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.
Brahma R; Raghuraman H
Emerg Top Life Sci; 2021 May; 5(1):89-101. PubMed ID: 33416893
[TBL] [Abstract][Full Text] [Related]
8. Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.
Kelkar DA; Chaudhuri A; Haldar S; Chattopadhyay A
Eur Biophys J; 2010 Sep; 39(10):1453-63. PubMed ID: 20372885
[TBL] [Abstract][Full Text] [Related]
9. Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.
Chakraborty H; Chattopadhyay A
J Fluoresc; 2017 Nov; 27(6):1995-2000. PubMed ID: 28687983
[TBL] [Abstract][Full Text] [Related]
10. Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems.
Mukherjee S; Chattopadhyay A
J Fluoresc; 1995 Sep; 5(3):237-46. PubMed ID: 24226791
[TBL] [Abstract][Full Text] [Related]
11. Tubulin conformation and dynamics: a red edge excitation shift study.
Guha S; Rawat SS; Chattopadhyay A; Bhattacharyya B
Biochemistry; 1996 Oct; 35(41):13426-33. PubMed ID: 8873611
[TBL] [Abstract][Full Text] [Related]
12. Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.
Mitra M; Chaudhuri A; Patra M; Mukhopadhyay C; Chakrabarti A; Chattopadhyay A
J Fluoresc; 2015 May; 25(3):707-17. PubMed ID: 25835748
[TBL] [Abstract][Full Text] [Related]
13. Solvation dynamics of a protein in the pre molten globule state.
Samaddar S; Mandal AK; Mondal SK; Sahu K; Bhattacharyya K; Roy S
J Phys Chem B; 2006 Oct; 110(42):21210-5. PubMed ID: 17048947
[TBL] [Abstract][Full Text] [Related]
14. Fluorophore environments in membrane-bound probes: a red edge excitation shift study.
Chattopadhyay A; Mukherjee S
Biochemistry; 1993 Apr; 32(14):3804-11. PubMed ID: 8466919
[TBL] [Abstract][Full Text] [Related]
15. Structural and dynamical insights into the molten-globule form of ovalbumin.
Bhattacharya M; Mukhopadhyay S
J Phys Chem B; 2012 Jan; 116(1):520-31. PubMed ID: 22097968
[TBL] [Abstract][Full Text] [Related]
16. Monitoring gramicidin conformations in membranes: a fluorescence approach.
Rawat SS; Kelkar DA; Chattopadhyay A
Biophys J; 2004 Aug; 87(2):831-43. PubMed ID: 15298892
[TBL] [Abstract][Full Text] [Related]
17. Studies of the molten globule state of ferredoxin: structural characterization and implications on protein folding and iron-sulfur center assembly.
Leal SS; Gomes CM
Proteins; 2007 Aug; 68(3):606-16. PubMed ID: 17510960
[TBL] [Abstract][Full Text] [Related]
18. Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.
Warrender AK; Pan J; Pudney C; Arcus VL; Kelton W
J R Soc Interface; 2023 Nov; 20(208):20230337. PubMed ID: 37935360
[TBL] [Abstract][Full Text] [Related]
19. Location, dynamics and solvent relaxation of a Nile Red-based phase-sensitive fluorescent membrane probe.
Saxena R; Shrivastava S; Haldar S; Klymchenko AS; Chattopadhyay A
Chem Phys Lipids; 2014 Oct; 183():1-8. PubMed ID: 24802972
[TBL] [Abstract][Full Text] [Related]
20. Fluorescence spectroscopy.
Royer CA
Methods Mol Biol; 1995; 40():65-89. PubMed ID: 7633532
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
