D. Amir

发表

Fast collapse but slow formation of secondary structure elements in the refolding transition of E. coli adenylate kinase.

E. Haas, V. Ratner, D. Amir, 2005, Journal of molecular biology.

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

E. Haas, D. Amir, E. Lerner, 2014, Methods in molecular biology.

Early closure of a long loop in the refolding of adenylate kinase: a possible key role of non-local interactions in the initial folding steps.

Elisha Haas, Tomer Orevi, E. Haas, 2009, Journal of molecular biology.

Fast subdomain folding prior to the global refolding transition of E. coli adenylate kinase: a double kinetics study.

Elisha Haas, Tomer Orevi, Gil Rahamim, 2012, Journal of molecular biology.

Modulation of functionally significant conformational equilibria in adenylate kinase by high concentrations of trimethylamine oxide attributed to volume exclusion.

Elisha Haas, A. Minton, D. Goldenberg, 2011, Biophysical journal.

Bio-inspired Photocatalytic Ruthenium Complexes: Synthesis, Optical Properties, and Solvatochromic Effect.

D. Amir, Yuval Elias, A. Salomon, 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

The cationic dye basic orange 21 (BO21) as a potential fluorescent sensor

D. Amir, N. Zurgil, M. Deutsch, 2018, Photochemical and Photobiological Sciences.

Reduced bovine pancreatic trypsin inhibitor has a compact structure.

E. Haas, D. Amir, D Amir, 1988, Biochemistry.

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

E. Haas, D. Amir, 1987, Biochemistry.

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

E. Haas, D. Amir, 1986, Biopolymers.

Inherited Human Sex Reversal due to Loss of a Water-Mediated Hydrogen Bond at a Conserved Protein-DNA Interface

E. Haas, D. Amir, M. Weiss, 2021, bioRxiv.

Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.

E. Haas, D. Amir, G. Rahamim, 2017, Biophysical journal.

Fast closure of long loops at the initiation of the folding transition of globular proteins studied by time-resolved FRET-based methods

Dan Amir, Elisha Haas, Tomer Orevi, 2014, Bio Algorithms Med Syst..

Early Closure of Loops in the Refolding of Adenylate Kinase: A Possible Key Role for Non Local Interactions in the Initial Folding Steps

Elisha Haas, Tomer Orevi, Gil Rahamim, 2009 .

Preparation of homogeneous samples of double-labelled protein suitable for single-molecule FRET measurements

Y. Garini, E. Haas, D. Amir, 2013, Analytical and Bioanalytical Chemistry.

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.

E. Haas, D. Amir, G. Rahamim, 2012, The Review of scientific instruments.

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

A. Fersht, E. Haas, D. Amir, 2009, Biochemistry.

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

C. Matthews, E. Haas, O. Bilsel, 2016, Biochemistry.

Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements

Elisha Haas, Gil Rahamim, E. Haas, 2015, PloS one.

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

E. Haas, D. Amir, T. Orevi, 2014, Biochemistry.

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

E. Haas, D. Amir, E. Lerner, 2014, Biophysical journal.

The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways

E. Haas, D. Amir, T. Orevi, 2013, Biophysical Reviews.

Predicting reactivities of protein surface cysteines as part of a strategy for selective multiple labeling.

Elisha Haas, E. Haas, V. Ratner, 2005, Biochemistry.

Using fluorescence correlation spectroscopy to study conformational changes in denatured proteins.

Yosef Y. Kuttner, E. Haas, D. Amir, 2008, Biophysical journal.

Detection of local structures in reduced unfolded bovine pancreatic trypsin inhibitor

E. Haas, S. Krausz, D. Amir, 1992, Proteins.

Selective fluorescent labeling at the α‐amino group of bovine pancreatic trypsin inhibitor

E. Haas, D. Amir, Lidya Varshavski, 1985 .

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

E. Haas, D. Amir, E. Kahana, 2004, Journal of molecular recognition : JMR.