Geometric phaselike effects in a quantum heat engine

By periodically driving the temperatures of reservoirs in quantum heat engines, geometric phase or Pancharatnam-Berry phase-like (PBp) effects in the thermodynamics can be observed. The PBp can be identified from a generating function (GF) method within an adiabatic quantum Markovian master equation formalism. The GF is shown not to lead to a standard open quantum system's fluctuation theorem in presence of phase-different modulations with an inapplicability in the use of the popular large deviation theory. Effect of coherences on the optimized value of the flux is nullified due to PBp contributions. The PBp causes the universality of the linear coefficient in the expansion of the efficiency at maximum power in terms of Carnot efficiency to be violated.Comment: 8 pages, 4 figure

Toward an Alternative Intrinsic Probe for Spectroscopic Characterization of a Protein

The intrinsic fluorescent amino acid tryptophan is the unanimous choice for the spectroscopic investigation of proteins. However, several complicacies in the interpretation of tryptophan fluorescence in a protein are inevitable and an alternative intrinsic protein probe is a longstanding demand. In this contribution, we report an electron-transfer reaction in a human transporter protein (HSA) cavity which causes the tryptophan residue (Trp214) to undergo chemical modification to form one of its metabolites kynurenine (Kyn214). Structural integrity upon modification of the native protein is confirmed by dynamic light scattering (DLS) as well as near and far circular dichroism (CD) spectroscopy. Femtosecond-resolved fluorescence transients of the modified protein describe the dynamics of solvent molecules in the protein cavity in both the native and denatured states. In order to establish general use of the probe, we have studied the dipolar interaction of Kyn214 with a surface-bound ligand (crystal violet, CV) of the protein. By using the sensitivity of FRET, we have determined the distance between Kyn214 (donor) and CV (acceptor). Our study is an attempt to explore an alternative intrinsic fluorescence probe for the spectroscopic investigation of a protein. In order to establish the efficacy of the modification technique we have converted the tryptophan residues of other proteins (bovine serum albumin, chymotrypsin and subtilisin Carlsberg) to kynurenine and confirmed their structural integrity. We have also shown that catalytic activity of the enzymes remains intact upon the modification