Roder H - Search Results

1

Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg].

Dlott DD, Frauenfelder H, Langer P, Roder H, DiIorio EE. Dlott DD, et al. Among authors: roder h. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6239-43. doi: 10.1073/pnas.80.20.6239. Proc Natl Acad Sci U S A. 1983. PMID: 6578506 Free PMC article.

2

Ligand binding to heme proteins: relevance of low-temperature data.

Ansari A, DiIorio EE, Dlott DD, Frauenfelder H, Iben IE, Langer P, Roder H, Sauke TB, Shyamsunder E. Ansari A, et al. Among authors: roder h. Biochemistry. 1986 Jun 3;25(11):3139-46. doi: 10.1021/bi00359a011. Biochemistry. 1986. PMID: 3730353

3

Comparison of the magnetic properties of deoxy- and photodissociated myoglobin.

Roder H, Berendzen J, Bowne SF, Frauenfelder H, Sauke TB, Shyamsunder E, Weissman MB. Roder H, et al. Proc Natl Acad Sci U S A. 1984 Apr;81(8):2359-63. doi: 10.1073/pnas.81.8.2359. Proc Natl Acad Sci U S A. 1984. PMID: 6585802 Free PMC article.

4

Fast events in protein folding initiated by nanosecond laser photolysis.

Jones CM, Henry ER, Hu Y, Chan CK, Luck SD, Bhuyan A, Roder H, Hofrichter J, Eaton WA. Jones CM, et al. Among authors: roder h. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11860-4. doi: 10.1073/pnas.90.24.11860. Proc Natl Acad Sci U S A. 1993. PMID: 8265638 Free PMC article.

5

Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein.

Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F. Zhu Y, et al. Among authors: roder h. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15486-91. doi: 10.1073/pnas.2136623100. Epub 2003 Dec 11. Proc Natl Acad Sci U S A. 2003. PMID: 14671331 Free PMC article.

6

A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale.

Shastry MC, Luck SD, Roder H. Shastry MC, et al. Among authors: roder h. Biophys J. 1998 May;74(5):2714-21. doi: 10.1016/S0006-3495(98)77977-9. Biophys J. 1998. PMID: 9591695 Free PMC article.

7

Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

Roder H, Wagner G, Wüthrich K. Roder H, et al. Biochemistry. 1985 Dec 3;24(25):7396-407. doi: 10.1021/bi00346a055. Biochemistry. 1985. PMID: 2417625

Biochem. 145, 431-436] and for more detailed investigations of the intrinsic exchange rates for solvent-exposed amide protons in the "open" states of a protein [Roder, H., Wagner, G., & Wuthrich, K. (1985) Biochemistry (following paper in this issue)]....

Biochem. 145, 431-436] and for more detailed investigations of the intrinsic exchange rates for solvent-exposed amide protons in the "open" …

8

Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.

Hagen SJ, Latypov RF, Dolgikh DA, Roder H. Hagen SJ, et al. Among authors: roder h. Biochemistry. 2002 Jan 29;41(4):1372-80. doi: 10.1021/bi011371a. Biochemistry. 2002. PMID: 11802740

9

Internal friction controls the speed of protein folding from a compact configuration.

Pabit SA, Roder H, Hagen SJ. Pabit SA, et al. Among authors: roder h. Biochemistry. 2004 Oct 5;43(39):12532-8. doi: 10.1021/bi048822m. Biochemistry. 2004. PMID: 15449942

10

Identification of the predominant non-native histidine ligand in unfolded cytochrome c.

Colón W, Wakem LP, Sherman F, Roder H. Colón W, et al. Among authors: roder h. Biochemistry. 1997 Oct 14;36(41):12535-41. doi: 10.1021/bi971697c. Biochemistry. 1997. PMID: 9376358

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