Refolding of β-lactoglobulin studied by stopped-flow circular dichroism at subzero temperatures-Reference-Cited by-同舟云学术

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Refolding of β-lactoglobulin studied by stopped-flow circular dichroism at subzero temperatures

Published:2001-11-02 Issue:3 Volume:507 Page:299-302
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Qin Zhi-jie,Hu Dong-mei,Shimada Lui,Nakagawa Tatsuo,Arai Munehito,Zhou Jun-Mei,Kihara Hiroshi

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(01)02886-1/fullpdf

Reference19 articles.

1. Molten Globule and Protein Folding

2. Role of the molten globule state in protein folding

3. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism

4. The Burst-phase Intermediate in the Refolding of β-Lactoglobulin Studied by Stopped-flow Circular Dichroism and Absorption Spectroscopy

5. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy 1 1Edited by P. E. Wright

Cited by 15 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Protein flexibility and cryoenzymology: the trade-off between stability and catalytic rates;Structure and Intrinsic Disorder in Enzymology;2023

2. The effect of surface charge on the thermal stability and ice recrystallization inhibition activity of antifreeze protein III (AFP III);Biochemical and Biophysical Research Communications;2018-01

3. Transient Non-Native Helix Formation during the Folding of β-Lactoglobulin;Biomolecules;2014-02-13

4. α-helix formation rate of oligopeptides at subzero temperatures;BIOPHYSICS;2014

5. Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering;Biophysical Chemistry;2013-05

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