Linear Chromatic Adaptation Transform Based on Delaunay Triangulation

Computer vision algorithms that use color information require color constant images to operate correctly. Color constancy of the images is usually achieved in two steps: first the illuminant is detected and then image is transformed with the chromatic adaptation transform ( CAT). Existing CAT methods use a single transformation matrix for all the colors of the input image. The method proposed in this paper requires multiple corresponding color pairs between source and target illuminants given by patches of the Macbeth color checker. It uses Delaunay triangulation to divide the color gamut of the input image into small triangles. Each color of the input image is associated with the triangle containing the color point and transformed with a full linear model associated with the triangle. Full linear model is used because diagonal models are known to be inaccurate if channel color matching functions do not have narrow peaks. Objective evaluation showed that the proposed method outperforms existing CAT methods by more than 21%; that is, it performs statistically significantly better than other existing methods.

Energetics and Structural Characterization of the large-scale Functional Motion of Adenylate Kinase

Adenylate Kinase (AK) is a signal transducing protein that regulates cellular energy homeostasis balancing between different conformations. An alteration of its activity can lead to severe pathologies such as heart failure, cancer and neurodegenerative diseases. A comprehensive elucidation of the large-scale conformational motions that rule the functional mechanism of this enzyme is of great value to guide rationally the development of new medications. Here using a metadynamics-based computational protocol we elucidate the thermodynamics and structural properties underlying the AK functional transitions. The free energy estimation of the conformational motions of the enzyme allows characterizing the sequence of events that regulate its action. We reveal the atomistic details of the most relevant enzyme states, identifying residues such as Arg119 and Lys13, which play a key role during the conformational transitions and represent druggable spots to design enzyme inhibitors. Our study offers tools that open new areas of investigation on large-scale motion in proteins.