Retinal location and structure in squid rhodopsin

In order to understand retinal we calculated the dihedral angles around carbon axis IOC-12C, since two different carbon sequences 9C-10C-11C-12C and 10C-11C-12C-13C exist. We also calculated the distances between two specified carbon pairs. Those results are tabulated. Photon absorption changes the conformation of retinal conformation. This fact is confirmed from dihedral angle changes and distance changes of targeted of retinal carbon atoms. These matters are discussed in the present paper.Copyright Information: Copyright the autho

Using Benthic Imagery to Assess the Coral Reef Community around Wake Atoll

OCN 499 - Undergraduate Thesi

Atomic configuration around retinal in squid rhodopsin

Distances among retinal carbons and amino acid residues around a retinal molecule are calculated. We draw an image for chain-A and chain-B contact with squid retinal. Thus the area of each retinal's chain-A and chain-B is decided in an average sense that is not exact. We discuss about distances and determined areas of retinals

Mass Spectrometry-Based Approaches Toward Absolute Quantitative Proteomics

Mass spectrometry has served as a major tool for the discipline of proteomics to catalogue proteins in an unprecedented scale. With chemical and metabolic techniques for stable isotope labeling developed over the past decade, it is now routinely used as a method for relative quantification to provide valuable information on alteration of protein abundance in a proteome-wide scale. More recently, absolute or stoichiometric quantification of proteome is becoming feasible, in particular, with the development of strategies with isotope-labeled standards composed of concatenated peptides. On the other hand, remarkable progress has been also made in label-free quantification methods based on the number of identified peptides. Here we review these mass spectrometry-based approaches for absolute quantification of proteome and discuss their implications