Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study

Pramana ◽  
2004 ◽  
Vol 63 (2) ◽  
pp. 363-368 ◽  
Author(s):  
Amit Das ◽  
R. Chitra ◽  
R. R. Choudhury ◽  
M. Ramanadham



Langmuir ◽  
2019 ◽  
Vol 35 (34) ◽  
pp. 11210-11216
Author(s):  
Sofiya Matviykiv ◽  
Hans Deyhle ◽  
Joachim Kohlbrecher ◽  
Frederik Neuhaus ◽  
Andreas Zumbuehl ◽  
...  


2017 ◽  
Vol 29 (2) ◽  
pp. 101-113 ◽  
Author(s):  
Osita Sunday Nnyigide ◽  
Yuna Oh ◽  
Hyeong Yong Song ◽  
Eun-kyoung Park ◽  
Soo-Hyung Choi ◽  
...  


2021 ◽  
Vol 83 (2) ◽  
pp. 117-123
Author(s):  
Arum Patriati ◽  
Edy Giri Rachman Putra

The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.



2018 ◽  
Author(s):  
James I Austerberry ◽  
Daniel J Belton

AbstractThe rapid and complex nature of protein aggregation makes the identification of aggregation mechanisms and their precursors challenging. Here we demonstrate the novel use of small-angle neutron scattering to perform dynamic real-time measurement and analysis of protein aggregation. Changes in bovine serum albumin monomer population and aggregate size are identified at several isothermal temperatures. Kratky plots indicate that the aggregation of BSA occurs through the partial unfolding of the monomer. Dual population modelling of the scattering data indicates that the protein nucleates and grows through a two stage mechanism; a rapid burst phase and a slower growth phase. Both stages are observed to follow Arrhenius behaviour between 70-80 °C.



Pramana ◽  
2008 ◽  
Vol 71 (5) ◽  
pp. 1027-1031 ◽  
Author(s):  
Nuzhat Gull ◽  
S. Chodankar ◽  
V. K. Aswal ◽  
Kabir-Ud-Din


2004 ◽  
Vol 120 (13) ◽  
pp. 6197-6206 ◽  
Author(s):  
Markus Stieger ◽  
Walter Richtering ◽  
Jan Skov Pedersen ◽  
Peter Lindner


2008 ◽  
Vol 155 (2) ◽  
pp. 80-89 ◽  
Author(s):  
Daniela Uhríková ◽  
Norbert Kučerka ◽  
José Teixeira ◽  
Valentin Gordeliy ◽  
Pavol Balgavý


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