Amir D - Search Results

1

Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A.

Huang F, Lerner E, Sato S, Amir D, Haas E, Fersht AR. Huang F, et al. Among authors: amir d. Biochemistry. 2009 Apr 21;48(15):3468-76. doi: 10.1021/bi801890w. Biochemistry. 2009. PMID: 19222162

2

Applications of time-resolved resonance energy transfer measurements in studies of the molecular crowding effect.

Ittah V, Kahana E, Amir D, Haas E. Ittah V, et al. Among authors: amir d. J Mol Recognit. 2004 Sep-Oct;17(5):448-55. doi: 10.1002/jmr.702. J Mol Recognit. 2004. PMID: 15362104

3

Ensemble and single-molecule detected time-resolved FRET methods in studies of protein conformations and dynamics.

Orevi T, Lerner E, Rahamim G, Amir D, Haas E. Orevi T, et al. Among authors: amir d. Methods Mol Biol. 2014;1076:113-69. doi: 10.1007/978-1-62703-649-8_7. Methods Mol Biol. 2014. PMID: 24108626

4

Fast closure of N-terminal long loops but slow formation of β strands precedes the folding transition state of Escherichia coli adenylate kinase.

Orevi T, Ben Ishay E, Gershanov SL, Dalak MB, Amir D, Haas E. Orevi T, et al. Among authors: amir d. Biochemistry. 2014 May 20;53(19):3169-78. doi: 10.1021/bi500069w. Epub 2014 May 12. Biochemistry. 2014. PMID: 24787383

5

Sequential Closure of Loop Structures Forms the Folding Nucleus during the Refolding Transition of the Escherichia coli Adenylate Kinase Molecule.

Orevi T, Rahamim G, Amir D, Kathuria S, Bilsel O, Matthews CR, Haas E. Orevi T, et al. Among authors: amir d. Biochemistry. 2016 Jan 12;55(1):79-91. doi: 10.1021/acs.biochem.5b00849. Epub 2015 Dec 23. Biochemistry. 2016. PMID: 26666584

6

Estimation of intramolecular distance distributions in bovine pancreatic trypsin inhibitor by site-specific labeling and nonradiative excitation energy-transfer measurements.

Amir D, Haas E. Amir D, et al. Biochemistry. 1987 Apr 21;26(8):2162-75. doi: 10.1021/bi00382a015. Biochemistry. 1987. PMID: 2441742

7

Reduced bovine pancreatic trypsin inhibitor has a compact structure.

Amir D, Haas E. Amir D, et al. Biochemistry. 1988 Dec 13;27(25):8889-93. doi: 10.1021/bi00425a003. Biochemistry. 1988. PMID: 2466482

The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradiative excitation energy-transfer efficiencies (E) between a donor probe attached to the N-terminal Arg1 residue and an acceptor attached to o …

The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradia …

8

Kinetics of fast changing intramolecular distance distributions obtained by combined analysis of FRET efficiency kinetics and time-resolved FRET equilibrium measurements.

Lerner E, Orevi T, Ben Ishay E, Amir D, Haas E. Lerner E, et al. Among authors: amir d. Biophys J. 2014 Feb 4;106(3):667-76. doi: 10.1016/j.bpj.2013.11.4500. Biophys J. 2014. PMID: 24507607 Free PMC article.

9

An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for "double kinetics" experiments: application to fluorescence resonance excitation energy transfer study of protein folding.

Ishay EB, Hazan G, Rahamim G, Amir D, Haas E. Ishay EB, et al. Among authors: amir d. Rev Sci Instrum. 2012 Aug;83(8):084301. doi: 10.1063/1.4737632. Rev Sci Instrum. 2012. PMID: 22938314

10

Determination of intramolecular distance distributions in a globular protein by nonradiative excitation energy transfer measurements.

Amir D, Haas E. Amir D, et al. Biopolymers. 1986 Feb;25(2):235-40. doi: 10.1002/bip.360250205. Biopolymers. 1986. PMID: 2420384 No abstract available.

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