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Genetics of proteins

This theory proposed by Beadle and Tatum (1941) implied that the structure of an enzyme or a protein is controlled by one gene, in the sense that one gene encodes one protein. This theory became useful in understanding [Pg.9]

this theory became useful in establishing the identification of a particular protein and its role in a biochemical step in the metabolic pathway by [Pg.11]

2 Protein as a Sequence of Amino Acids. The fact that a protein is a sequence an amino acid was directly established by the elucidation of the structure of insulin polypeptide as a linear sequence of different amino acids by Sanger (1958). Thus, insulin was the polypeptide or a small protein that was sequenced first by Sanger (1958). Ribonucle-ase A was the first full-size protein and an enzyme that was sequenced by [Pg.13]

The one-gene-one-enzyme concept did imply that the primary structure of the peptide determines the secondary, tertiary, and quaternary structure, and this was established by Anhnsen (1973) by an analysis of the mutant ribonuclease and by the study of chemical modification as well as the denaturation and renaturation kinetics of this enzyme (Anhnsen 1973). [Pg.14]

The central dogma of biology suggests the direction of the flow of genetic information from DNA to RNA to protein is DNA - RNA —Protein. [Pg.14]


It had often been assumed that a hydrophobic signal sequence, perhaps folded into a hairpin loop, spontaneously inserts itself into an ER membrane to initiate translocation. However, study of the genetics of protein transport suggests otherwise. Over 50 different genetic loci affect the translocation of proteins in yeast.31/32/33d Products of these secretory genes,... [Pg.520]

Klimov D K and Thirumalai D 1996 Factors governing the foldability of proteins Proteins Struct. Funct. Genet. 26 411-41... [Pg.2665]

S. Sun, Reduced representation model of protein structure prediction statistical potential and genetic algorithms. Protein Sci. 2 (1993), 762-785. [Pg.223]

Bryngelson J D, J N Onuchic, N D Socci and P G Wolynes 1995. Funnels, Pathways, and the Energy Landscape of Protein Folding A Synthesis. Proteins Structure, Function and Genetics 21 167-195. [Pg.574]

Mosimann S, S Meleshko and M N G Jones 1995. A Critical Assessment of Comparative Molecular Modeling of Tertiary Structures of Proteins. Proteins Structure, Function and Genetics 23 301-317. [Pg.576]

Moult J, T Hubbard, K Fldelis and J T Pedersen 1999. Critical Assessment of Methods of Protein Structure Prediction (CASP) Round III. Proteins Structure, Function and Genetics Suppl. 3 2-6. [Pg.576]

Besides the worldwide WPI database, Derwent provides on the ORBIT system the USPatents database, a bibhographic file of patent front page and cl aim information for U.S. patents since 1971. Derwent also produces a biotechnology database, GENESEQ, that indexes sequence stmetures of proteins or nucleic acids disclosed specifically or genetically in patents. This database is searchable with special sequence software on the InteUiGenetics system, and is a new addition to STN s database catalog. [Pg.54]

Thaumatin. Thaumatin [53850-34-3] is a mixture of proteins extracted from the fmit of a West African plant, Thaumatococcus daniellii (Beimett) Benth. Work at Unilever showed that the aqueous extract contains two principal proteins thaumatin I and thaumatin II. Thaumatin I, mol wt 22,209, contains 207 amino acids in a single chain that is cross-linked with eight disulfide bridges. Thaumatin II has the same number of amino acids, but there are five sequence differences. Production of thaumatins via genetic engineering technology has been reported (99). [Pg.281]

Research and clinical experience on dmg resistance suggests that tumor cells are particularly adept at genetic selections leading to alterations in the stmcture, function, or synthesis of proteins involved in the antitumor dmg action and detoxification. Multiple mechanisms of resistance have been shown to account for the resistance seen in the clinic (46). [Pg.445]

JU Bowie, ND Clarke, CO Paho, RT Sauer. Identification of protein folds Matching hydro-phohicity patterns of sequence sets with solvent accessibility patterns of known structures. Proteins Struct Func Genet 7 257-264, 1990. [Pg.346]

Koch, I., Kaden, R, Selbig, J. Analysis of protein sheet topologies by graph theoretical methods. Prot Struc. Func. Genet. 12 314-323, 1992. [Pg.33]

Two basic principles govern the arrangement of protein subunits within the shells of spherical viruses. The first is specificity subunits must recognize each other with precision to form an exact interface of noncovalent interactions because virus particles assemble spontaneously from their individual components. The second principle is genetic economy the shell is built up from many copies of a few kinds of subunits. These principles together imply symmetry specific, repeated bonding patterns of identical building blocks lead to a symmetric final structure. [Pg.327]


See other pages where Genetics of proteins is mentioned: [Pg.325]    [Pg.363]    [Pg.9]    [Pg.9]    [Pg.11]    [Pg.13]    [Pg.15]    [Pg.17]    [Pg.19]    [Pg.325]    [Pg.363]    [Pg.9]    [Pg.9]    [Pg.11]    [Pg.13]    [Pg.15]    [Pg.17]    [Pg.19]    [Pg.3035]    [Pg.129]    [Pg.148]    [Pg.534]    [Pg.578]    [Pg.578]    [Pg.42]    [Pg.206]    [Pg.247]    [Pg.249]    [Pg.171]    [Pg.87]    [Pg.248]    [Pg.194]    [Pg.205]    [Pg.206]    [Pg.120]    [Pg.78]    [Pg.394]    [Pg.144]    [Pg.178]    [Pg.285]    [Pg.328]    [Pg.57]    [Pg.300]    [Pg.300]   
See also in sourсe #XX -- [ Pg.9 ]




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