Structure of a partially unfolded form of E scherichia coli dihydrofolate reductase provides insight into its folding pathway-Reference-Cited by-同舟云学术

Structure of a partially unfolded form of E scherichia coli dihydrofolate reductase provides insight into its folding pathway

Published:2014-10-18 Issue:12 Volume:23 Page:1728-1737
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kasper Joseph R.¹,Liu Pei-Fen¹,Park Chiwook¹

Affiliation:

1. Department of Medicinal Chemistry and Molecular Pharmacology; Bindley Bioscience Center, Purdue University; West Lafayette Indiana 47907

Funder

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2555/fullpdf

Reference41 articles.

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3. Folding of dihydrofolate reductase from Escherichia coli;Touchette;Biochemistry,1986

4. Structure, dynamics, and catalytic function of dihydrofolate reductase;Schnell;Ann Rev Biophys Biomol Struct,2004

5. Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites;Frieden;Proc Natl Acad Sci USA,1990

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