Journal
JOURNAL OF PHYSICAL CHEMISTRY C
Volume 122, Issue 27, Pages 15567-15574Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcc.8b04356
Keywords
-
Funding
- JSPS KAKENHI Grant [JP16H04160, 17K19022, 15H03841]
- NSF [DMR-0520547]
- European Union's Horizon 2020 research and innovation program under the SINE2020 project [654000]
Ask authors/readers for more resources
In the present study, we examined the secondary and tertiary structure of myoglobin (Mb) within folded sheets mesoporous material (FSM)- and Santa Barbara amorphous (SBA)-type mesoporous silicas. The Barrett-Joyner-Halenda pore diameters of SBA-type mesoporous silicas were 39, 70, and 75 angstrom, and that of FSM-type mesoporous silica was 40 angstrom. The secondary and tertiary structures of myoglobin were observed by Fourier transform infrared (FTIR) and small-angle neutron scattering (SANS), respectively. The FTIR and SANS results indicated preservation of the secondary and tertiary structures of myoglobin inside the pores of SBA-type mesoporous silicas. Adsorption of myoglobin within FSM-type mesoporous silica, however, resulted in perturbation of the tertiary structure, accompanied by partial unfolding of the secondary structure. Lower structural stability of myoglobin within the FSM-type mesoporous silica was also confirmed. These findings suggest that the Mb structure is more influenced by the inner pore surface characteristics than by geometrical pore size.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available