Frieden C - Search Results

1

Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR.

Li H, Frieden C. Li H, et al. Among authors: frieden c. Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11993-8. doi: 10.1073/pnas.0705253104. Epub 2007 Jul 5. Proc Natl Acad Sci U S A. 2007. PMID: 17615232 Free PMC article.

2

Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.

Ropson IJ, Frieden C. Ropson IJ, et al. Among authors: frieden c. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7222-6. doi: 10.1073/pnas.89.15.7222. Proc Natl Acad Sci U S A. 1992. PMID: 1496015 Free PMC article.

3

Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.

Frieden C. Frieden C. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4413-6. doi: 10.1073/pnas.87.12.4413. Proc Natl Acad Sci U S A. 1990. PMID: 2191290 Free PMC article.

4

Folding of a predominantly beta-structure protein: rat intestinal fatty acid binding protein.

Ropson IJ, Gordon JI, Frieden C. Ropson IJ, et al. Among authors: frieden c. Biochemistry. 1990 Oct 16;29(41):9591-9. doi: 10.1021/bi00493a013. Biochemistry. 1990. PMID: 2271603

5

Actin polymerization induces a shape change in actin-containing vesicles.

Cortese JD, Schwab B 3rd, Frieden C, Elson EL. Cortese JD, et al. Among authors: frieden c. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5773-7. doi: 10.1073/pnas.86.15.5773. Proc Natl Acad Sci U S A. 1989. PMID: 2548187 Free PMC article.

6

Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein.

Hall JG, Frieden C. Hall JG, et al. Among authors: frieden c. Proc Natl Acad Sci U S A. 1989 May;86(9):3060-4. doi: 10.1073/pnas.86.9.3060. Proc Natl Acad Sci U S A. 1989. PMID: 2654934 Free PMC article.

7

Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.

Hoeltzli SD, Frieden C. Hoeltzli SD, et al. Among authors: frieden c. Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9318-22. doi: 10.1073/pnas.92.20.9318. Proc Natl Acad Sci U S A. 1995. PMID: 7568125 Free PMC article.

8

Intestinal fatty acid binding protein: folding of fluorescein-modified proteins.

Frieden C, Jiang N, Cistola DP. Frieden C, et al. Biochemistry. 1995 Feb 28;34(8):2724-30. doi: 10.1021/bi00008a040. Biochemistry. 1995. PMID: 7873555

In a previous report, six site-directed mutants were obtained, each having a single cysteine residue [Jiang, N., & Frieden, C., (1993) Biochemistry 32, 11015-11021] either in a turn or pointed into the cavity. ...

In a previous report, six site-directed mutants were obtained, each having a single cysteine residue [Jiang, N., & Frieden, C …

9

19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.

Hoeltzli SD, Frieden C. Hoeltzli SD, et al. Among authors: frieden c. Biochemistry. 1994 May 10;33(18):5502-9. doi: 10.1021/bi00184a019. Biochemistry. 1994. PMID: 8180172

10

Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues.

Jiang N, Frieden C. Jiang N, et al. Among authors: frieden c. Biochemistry. 1993 Oct 19;32(41):11015-21. doi: 10.1021/bi00092a010. Biochemistry. 1993. PMID: 8218166

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