Elucidation of μs dynamics of domain-III of human serum albumin during the chemical and thermal unfolding: A fluorescence correlation spectroscopic investigation

Sengupta, Bhaswati; Das, Nilimesh; Sen, Pratik

doi:10.1016/j.bpc.2016.11.006

Cited by 15 publications

(32 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The additional fluctuation time component observed for native HSA is found to be ∼8.3 μs, which is assigned as the conformational fluctuation time of domain-III of HSA. 50 There is almost no change of this time component with the addition of dextran-6. For both dextran-40 and dextran-70, a gradual increase of conformational fluctuation time was observed, as shown in Figure 5.…”

Section: ■ Resultsmentioning

confidence: 95%

“…The detailed description of the set up can be found in our previous reports. 50,51,59,60 The excitation source is a 405 nm continuous wave laser (5 mW, Optoelectronics Tech. Co. Ltd., China).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…A home-built FCS set up has been used for the single molecular level fluorescent measurement. The detailed description of the set up can be found in our previous reports. ,,, The excitation source is a 405 nm continuous wave laser (5 mW, Optoelectronics Tech. Co. Ltd., China).…”

Section: Methodsmentioning

confidence: 99%

“…51,52 We have also studied the effect of thermal and chemical denaturation on the dynamics using the same technique. 50 In the present contribution, we have employed FCS to investigate the effect of crowders on the structural transition and conformational fluctuation dynamics and attempted to relate it to the activity of HSA inside the crowding milieu. For this purpose, we have selectively tagged tyrosine-411 residue located in domain-III of HSA by a fluorescent marker pnitrophenyl coumarin ester (NPCE).…”

mentioning

confidence: 99%

“…As this conformational motion of the proteins is uncorrelated, a bulk measurement cannot provide information about the dynamics, and one has to perform the single molecular level study. In our previous contributions, we have reported the conformational dynamics of domain-III of HSA has a time constant of 8 μs, and that of domain-I has a time scale of 27 μs using single molecular level fluorescence correlation spectroscopy (FCS). , We have also studied the effect of thermal and chemical denaturation on the dynamics using the same technique …”

mentioning

confidence: 99%

See 4 more Smart Citations

Structural, Functional, and Dynamical Responses of a Protein in a Restricted Environment Imposed by Macromolecular Crowding

Das

Sen

2018

Biochemistry

Self Cite

View full text Add to dashboard Cite

The intercellular environment is known to be very different from the environment where most of the elementary biological processes are studied in the laboratory. As a result, there was a considerable effort on cell mimicking either by confinement or by introducing macromolecular crowding. In the present study, dextran of varying sizes has been used to crowd the environment of a protein, human serum albumin (HSA), and its structure, dynamics, and activity were studied as a function of crowder concentration. By employing bulk and single molecular level spectroscopic measurements, we elucidate the overall structure and local microsecond dynamics of HSA. Further, we have attempted to correlate these structural changes with its activity.

show abstract

Section: ■ Resultsmentioning

confidence: 95%