Analysis and Control of Protein Crystallization Using Short Peptide Tags That Change Solubility without Affecting Structure, Thermal Stability, and Function-Reference-Cited by-同舟云学术

Analysis and Control of Protein Crystallization Using Short Peptide Tags That Change Solubility without Affecting Structure, Thermal Stability, and Function

Published:2015-05-08 Issue:6 Volume:15 Page:2703-2711
ISSN:1528-7483
Container-title:Crystal Growth & Design
language:en
Short-container-title:Crystal Growth & Design

Author:

Islam Mohammad Monirul¹,Nakamura Shigeyoshi²,Noguchi Keiichi,Yohda Masafumi,Kidokoro Shun-ichi²,Kuroda Yutaka

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Chittagong, Chittagong 4331, Bangladesh

2. Department of Bioengineering, Nagaoka University of Technology, Niigata 940-2188, Japan

Funder

Ministry of Science and Technology, Government of the People's Republic of Bangladesh

Ministry of Education, Culture, Sports, Science, and Technology

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Condensed Matter Physics,General Materials Science,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.cgd.5b00010

Reference40 articles.

1. A Simple Method for Improving Protein Solubility and Long-Term Stability

2. Rational design of aggregation-resistant bioactive peptides: Reengineering human calcitonin

3. Structure-based substitutions for increased solubility of a designed protein

4. Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa

5. Making the most of affinity tags

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