Investigating the Refolding Pathway of Human Acidic Fibroblast Growth Factor (hFGF-1) from the Residual Structure(s) Obtained by Denatured-State Hydrogen/Deuterium Exchange-Reference-Cited by-同舟云学术

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Investigating the Refolding Pathway of Human Acidic Fibroblast Growth Factor (hFGF-1) from the Residual Structure(s) Obtained by Denatured-State Hydrogen/Deuterium Exchange

Published:2011-01 Issue:1 Volume:100 Page:154-164
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Wang Han-Min,Yu Chin

Publisher

Elsevier BV

Subject

Biophysics

Reference28 articles.

1. Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9;Li;J. Mol. Biol.,2005

2. Protein folding dynamics: the diffusion-collision model and experimental data;Karplus;Protein Sci.,1994

3. Persistence of native-like topology in a denatured protein in 8 M urea;Shortle;Science,2001

4. The molecular basis for the chemical denaturation of proteins by urea;Bennion;Proc. Natl. Acad. Sci. USA,2003

5. Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding;Wong;J. Mol. Biol.,2000

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1. DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science;Molecules;2022-06-10

2. Decoding an Amino Acid Sequence to Extract Information on Protein Folding;Molecules;2022-05-07

3. Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR;Biophysical Journal;2020-11

4. Suramin derivatives play an important role in blocking the interaction between FGF1 and FGFRD2 to inhibit cell proliferation;European Journal of Medicinal Chemistry;2020-11

5. Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR;2018-09-27

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