The human genome holds an extraordinary trove of information about human development, physiology, medicine and evolution. Here we report the results of an international collaboration to produce and make freely available a draft sequence of the human genome. We also present an initial analysis of the data, describing some of the insights that can be gleaned from the sequence.

/pdf/initial-sequencing-and-analysis-of-the-human-genome-5dapk1rsx1.pdf

Initial sequencing and analysis of the human genome.

抗原变异可使得多种致病微生物易于逃避宿主免疫应答。表达在感染红细胞表面的恶性疟原虫红细胞表面蛋白1（PfPMP1）与感染红细胞、内皮细胞、树突状细胞以及胎盘的单个或多个受体作用，在黏附及免疫逃避中起关键的作用。每个单倍体基因组var基因家族编码约60种成员，通过启动转录不同的var基因变异体为抗原变异提供了分子基础。

疟原虫var基因转换速率变化导致抗原变异[英]／Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A

CHAPTER 24 – Evolution of Protein Molecules

Semiconductor nanocrystals were prepared for use as fluorescent probes in biological staining and diagnostics. Compared with conventional fluorophores, the nanocrystals have a narrow, tunable, symmetric emission spectrum and are photochemically stable. The advantages of the broad, continuous excitation spectrum were demonstrated in a dual-emission, single-excitation labeling experiment on mouse fibroblasts. These nanocrystal probes are thus complementary and in some cases may be superior to existing fluorophores.

https://science.sciencemag.org/content/sci/281/5385/2013.full.pdf

Semiconductor Nanocrystals as Fluorescent Biological Labels

Highly luminescent semiconductor quantum dots (zinc sulfide-capped cadmium selenide) have been covalently coupled to biomolecules for use in ultrasensitive biological detection. In comparison with organic dyes such as rhodamine, this class of luminescent labels is 20 times as bright, 100 times as stable against photobleaching, and one-third as wide in spectral linewidth. These nanometer-sized conjugates are water-soluble and biocompatible. Quantum dots that were labeled with the protein transferrin underwent receptor-mediated endocytosis in cultured HeLa cells, and those dots that were labeled with immunomolecules recognized specific antibodies or antigens.

http://science.sciencemag.org/content/sci/281/5385/2016.full.pdf

Quantum Dot Bioconjugates for Ultrasensitive Nonisotopic Detection

Compositions are provided comprising sets of fluorescent labels carrying pairs of donor and acceptor dye molecules, designed for efficient excitation of the donors at a single wavelength and emission from the acceptor in each of the pairs at different wavelengths. The different molecules having different donor-acceptor pairs can be modified to have substantially the same mobility under separation conditions, by varying the distance between the donor and acceptor in a given pair. Particularly, the fluorescent compositions find use as labels in sequencing nucleic acids.

Fluorescent labels and their use in separations

https://www.jbc.org/content/266/15/9535.full.pdf

Phycoerythrins of marine unicellular cyanobacteria. iii, sequence of a class ii phycoerythrin

Comparative Studies of the Enzymatic Properties of Novo and Carlsberg Subtilisins

Structural studies on phycobiliproteins II. C-phycocyanin: amino acid sequence of the beta subunit. Specific cleavage of the alpha subunit.

Phycobilisomes are macromolecular light-harvesting antenna complexes attached to the cytoplasmic face of the thylakoid membranes in cyanobacterial cells and red algal chloroplasts These complexes, of about 6000 to 8000 kDa, are made up entirely of proteins and contain 500 to 700 linear tetrapyrroles (bilins) responsible for the absorption of visible light Phycobiliproteins are the major components of the phycobilisome and make up about 85% of the mass of the complex Within the phycobiliproteins, the bilins are covalently attached to cysteinyl residues through thioether linkages Four different isomeric bilins—phycocyanobilin, phycobiliviolin, phycoerythrobilin, and phycourobilin—have been found in cyanobacterial and red algal phycobiliproteins Bilins are formed from biliverdin IXα by two sequential ferredoxin-mediated two-electron reduction steps followed by isomerization reactions Attachment of the bilin to the apo-α subunit of C-phycocyanin has been shown to involve the participation of the products of two genes (cpcE and cpcF) that are a part of the phycocyanin operon Phycobilisomes have two morphologically distinct domains: a core with allophycocyanin as the main component, and rods with phycocyanin and (sometimes) phycoerythrin or phycoerythrocyanin as the major components The assembly of the phycobilisomes is governed by the interaction of the phycobiliproteins with a family of polypeptides that determine site-specific assembly, the linker polypeptides Special structural features of the phycobilisome minimize random walk of excitation energy among the bilins and assure directional energy transfer towards the terminal energy acceptors in the phycobilisome The phycobilisomes of open ocean marine cyanobacteria and red algae are rich in phycobiliproteins which absorb strongly in the green region of the spectrum Adaptive adjustments to light intensity, light quality, and nutrient limitation are achieved in part through changes in size or composition of the rod substructures of the phycobilisome

Alexander N. Glazer

Papers

Fluorescent labels and their use in separations

Phycoerythrins of marine unicellular cyanobacteria. iii, sequence of a class ii phycoerythrin

Comparative Studies of the Enzymatic Properties of Novo and Carlsberg Subtilisins

Structural studies on phycobiliproteins II. C-phycocyanin: amino acid sequence of the beta subunit. Specific cleavage of the alpha subunit.

Adaptive Variations in Phycobilisome Structure