Protein, proteins history

Zimmer DB, Cornwall EH, Landar A, Song W. 1995. The S100 protein family history, function, and expression. Brain Res Bull 37(4) 417—429. 

Means GE, Feeney RE. Chemical modifications of proteins history and applications. Bioconjug. Chem. 1990 1 2-12. 

Water and Proteins Some History and Current Perspectives... 

In the past 15 years, electrospray ionization has become one of the most important ionization methods in mass spectrometry. It is the method of choice in the coupling of liquid chromatography (LC) and mass spectrometry (MS). By estimation, it is used in over 90% of all LC-MS applications. It is especially useful in the analysis of highly polar, ionic, and macromolecular analytes. In addition, electrospray ionization plays an important role in the characterization of biomacromolecules, especially peptides and proteins. History, principle, instrumentation, practical aspects, and application of electrospray ionization are discussed in this article. 

PROTEIN-PROTEIN DOCKING A Short History of Protein-Protein Docking Introducing Docking in the 1970s... 

The fir.-fit line of the file (see Figure 2-110) - the HEADER record - hold.s the moleculc. s classification string (columns 11-50), the deposition date (the date when the data were received by the PDB) in columns 51-59, and the PDB (Dcode for the molecule, which is unique within the Protein Data Bank, in columns 63-66. The second line - the TITLE record - contains the title of the experiment or the analysis that is represented in the entry. The subsequent records contain a more detailed description of the macromolecular content of the entiy (COMPND), the biological and/or chemical source ofeach biological molecule in the entiy (SOURCE), a set ofkeywords relevant to the entiy (KEYWDS). information about the experiment (EXPDTA), a list of people responsible for the contents of this entiy (.AUTHOR), a history of modifications made to this entiy since its release (REVDAT), and finally the primaiy literature citation that describes the experiment which resulted in the deposited dataset ()RNL). 

History. Methods for the fractionation of plasma were developed as a contribution to the U.S. war effort in the 1940s (2). Following pubHcation of a seminal treatise on the physical chemistry of proteins (3), a research group was estabUshed which was subsequendy commissioned to develop a blood volume expander for the treatment of military casualties. Process methods were developed for the preparation of a stable, physiologically acceptable solution of alburnin [103218-45-7] the principal osmotic protein in blood. Eady preparations, derived from equine and bovine plasma, caused allergic reactions when tested in humans and were replaced by products obtained from human plasma (4). Process studies were stiU being carried out in the pilot-plant laboratory at Harvard in December 1941 when the small supply of experimental product was mshed to Hawaii to treat casualties at the U.S. naval base at Pead Harbor. On January 5, 1942 the decision was made to embark on large-scale manufacture at a number of U.S. pharmaceutical plants (4,5). 

Amino acids are the main components of proteins. Approximately twenty amino acids are common constituents of proteins (1) and are called protein amino acids, or primary protein amino acids because they are found in proteins as they emerge from the ribosome in the translation process of protein synthesis (2), or natural amino acids. In 1820 the simplest amino acid, glycine, was isolated from gelatin (3) the most recendy isolated, of nutritional importance, is L-threonine which was found (4) in 1935 to be a growth factor of rats. The history of the discoveries of the amino acids has been reviewed... 

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