Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor
Abstract Human acidic fibroblast growth factor (hFGF1) is an all beta-sheet protein that is involved in the regulation of key cellular processes including cell proliferation and wound healing. hFGF1 is known to aggregate when subjected to thermal unfolding. In this study, we investigate the equilibr...
Main Authors: | Shilpi Agrawal, Vivek Govind Kumar, Ravi Kumar Gundampati, Mahmoud Moradi, Thallapuranam Krishnaswamy Suresh Kumar |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2021-08-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-021-95050-2 |
Similar Items
-
Effect of extension of the heparin binding pocket on the structure, stability, and cell proliferation activity of the human acidic fibroblast growth factor
by: Julie Eberle Davis, et al.
Published: (2018-03-01) -
The Saga of Endocrine FGFs
by: Phuc Phan, et al.
Published: (2021-09-01) -
A superior drug carrier – aponeocarzinostatin in partially unfolded state fully protects the labile antitumor enediyne
by: Huang Chiy-Mey, et al.
Published: (2009-05-01) -
Protein-Phospholipid Interactions in Nonclassical Protein Secretion: Problem and Methods of Study
by: David Neivandt, et al.
Published: (2013-02-01) -
Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding
by: Atsushi Mukaiyama, et al.
Published: (2009-03-01)