Roder H - Search Results

1

Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange.

Roder H. Roder H. Methods Enzymol. 1989;176:446-73. doi: 10.1016/0076-6879(89)76024-9. Methods Enzymol. 1989. PMID: 2811697 No abstract available.

2

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

Roder H, Elöve GA, Englander SW. Roder H, et al. Nature. 1988 Oct 20;335(6192):700-4. doi: 10.1038/335700a0. Nature. 1988. PMID: 2845279 Free PMC article.

3

Proton resonance assignments of horse ferrocytochrome c.

Wand AJ, Di Stefano DL, Feng YQ, Roder H, Englander SW. Wand AJ, et al. Among authors: roder h. Biochemistry. 1989 Jan 10;28(1):186-94. doi: 10.1021/bi00427a026. Biochemistry. 1989. PMID: 2539854

4

Proton resonance assignments of horse ferricytochrome c.

Feng Y, Roder H, Englander SW, Wand AJ, Di Stefano DL. Feng Y, et al. Among authors: roder h. Biochemistry. 1989 Jan 10;28(1):195-203. doi: 10.1021/bi00427a027. Biochemistry. 1989. PMID: 2539855

As starting points for the assignment of the oxidized protein, a limited set of protons was initially assigned by use of 2D NMR magnetization transfer methods to correlate resonances in the oxidized form with assigned resonances in the reduced form [Wand, A. J., Di Stefano, D. L. …

As starting points for the assignment of the oxidized protein, a limited set of protons was initially assigned by use of 2D NMR magnetizatio …

5

Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

Jeng MF, Englander SW, Elöve GA, Wand AJ, Roder H. Jeng MF, et al. Among authors: roder h. Biochemistry. 1990 Nov 20;29(46):10433-7. doi: 10.1021/bi00498a001. Biochemistry. 1990. PMID: 2176867 Review.

6

Early hydrogen-bonding events in the folding reaction of ubiquitin.

Briggs MS, Roder H. Briggs MS, et al. Among authors: roder h. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2017-21. doi: 10.1073/pnas.89.6.2017. Proc Natl Acad Sci U S A. 1992. PMID: 1312711 Free PMC article.

7

Structural and kinetic characterization of early folding events in beta-lactoglobulin.

Kuwata K, Shastry R, Cheng H, Hoshino M, Batt CA, Goto Y, Roder H. Kuwata K, et al. Among authors: roder h. Nat Struct Biol. 2001 Feb;8(2):151-5. doi: 10.1038/84145. Nat Struct Biol. 2001. PMID: 11175905

8

Watching protein folding unfold.

Roder H. Roder H. Nat Struct Biol. 1995 Oct;2(10):817-20. doi: 10.1038/nsb1095-817. Nat Struct Biol. 1995. PMID: 7552699

9

Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands.

Elöve GA, Bhuyan AK, Roder H. Elöve GA, et al. Among authors: roder h. Biochemistry. 1994 Jun 7;33(22):6925-35. doi: 10.1021/bi00188a023. Biochemistry. 1994. PMID: 8204626

The observation of a single highly protected (140-fold) backbone amide, that of His 18, suggests the presence of a persistent H-bond consistent with heme ligation of the His 18 side chain in the unfolded state. ...A fast kinetic phase (80 s-1) accompanied by a major decrea …

The observation of a single highly protected (140-fold) backbone amide, that of His 18, suggests the presence of a persistent H-bond …

10

Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding.

Colón W, Elöve GA, Wakem LP, Sherman F, Roder H. Colón W, et al. Among authors: roder h. Biochemistry. 1996 Apr 30;35(17):5538-49. doi: 10.1021/bi960052u. Biochemistry. 1996. PMID: 8611545

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