Confirmation of the formation of salt bridges in the denatured state of CutA1 protein using molecular dynamics simulations-Reference-Cited by-同舟云学术

Confirmation of the formation of salt bridges in the denatured state of CutA1 protein using molecular dynamics simulations

Published:2019 Issue:0 Volume:16 Page:176-184
ISSN:2189-4779
Container-title:Biophysics and Physicobiology
language:en
Short-container-title:BIOPHYSICS

Author:

Yutani Katsuhide¹,Matsuura Yoshinori¹,Joti Yasumasa¹²

Affiliation:

1. RIKEN SPring-8 Center

2. Japan Synchrotron Radiation Research Institute

Publisher

Biophysical Society of Japan

Subject

General Medicine

Link

https://www.jstage.jst.go.jp/article/biophysico/16/0/16_176/_pdf

Reference17 articles.

1. [2] Suhre, K. & Claverie, J.-M. Genomic correlates of hyperthermostability, an update. J. Biol. Chem. 278, 17198–17202 (2003).

2. [5] Karshikoff, A. & Ladenstein, R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a “traffic rule” for hot roads. Trends Biochem. Sci. 26, 550–557 (2001).

3. [7] Matsuura, Y., Takehira, M., Sawano, M., Ogasahara, K., Tanaka, T., Yamamoto, H., et al. Role of charged residues in stabilization of Pyrococcus horikoshii CutA1, which has a denaturation temperature of nearly 150°C. FEBS J. 279, 78–90 (2012).

4. [9] Sterner, R. & Liebl, W. Thermophilic adaptation of proteins. Crit. Rev. Biochem. Mol. Biol. 36, 39–106 (2001).

5. [12] Sadeghi, M., Naderi-Manesh, H., Zarrabi, M. & Ranjbar, B. Effective factors in thermostability of thermophilic proteins. Biophys. Chem. 119, 256–270 (2006).

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