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Protein building blocks

The analysis of extraterrestrial matter is concentrated on the detection of nucleic acid and protein building blocks, i.e., N-heterocycles and amino acids. The search for such compounds began immediately after the fall of the Murchison meteorite. Twenty-two amino acids were detected in it as early as 1974 eight of them pro-teinogenic, ten which hardly ever occurred in biological material, and four which were unknown in the biosphere. Up to now, about 70 amino acids have been identified (Cronin, 1998), the most common being glycine and a-aminoisobutyric acid. The latter is a branched-chain amino acid with the smallest possible number of carbon atoms. The most frequently found amino acids occur in concentrations of... [Pg.69]

Several institutes throughout the world immediately began to carry out experiments on prebiotic chemistry. At this point, we need to realize that the prebiotic synthesis of protein building blocks is only a first step towards solving the biogenesis problem. Put simply, it is a method for making bricks which will later be used in building a multi-storey office block ... [Pg.88]

X can be any of the four nucleobases—G, A, C or U thus, four anticodons can be formed GGC, GAC, GCC and GUC. The antiparallel structure contains the codons GCC, GUC, GGC and GAC. Today, these codons code for the four amino acids alanine, glycine, valine and aspartic acid. These are, astonishingly, the four protein building blocks produced in the best yields in the Miller-Urey experiment, and they... [Pg.220]

DNA. These types of RNA help assemble protein building blocks (amino acids) into functioning proteins. [Pg.14]

Deciphering amino acid structure and how these protein building blocks form... [Pg.281]

Raman difference spectroscopy has also been used to understand the molecular mechanism of viral core assemblies yielding information on viral subunits from precursor and mature states. Benevides et al. employed Raman difference spectroscopy to investigate conformational changes of the protein building blocks of the icosahedral core of a double-stranded RNA (p6 virus during viral procapsid and capsid assembly [18],... [Pg.442]

Meaning comprising three distinct protein building blocks. [Pg.100]

Mathys, S., Evans, T. C., Chute, I. C., et al. (1999) Characterization of a self-sphcing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements facile production of protein building blocks for protein ligation. Gene 231, 1—13. [Pg.127]

Electrochemically controlled SAMs of the alkanethiol class characterized to high voltammetric resolution and to molecular and sub-molecular structural in situ STM resolution have been reviewed recently [60, 151]. We note here first some issues of importance to functionalized alkanethiols as linker molecules for gentle immobilization of fully functional redox metalloprotein monolayers on singlecrystal Au(lll) electrode surfaces. We discuss next specifically the functionalized alkanethiols cysteine (Cys) and homocysteine (Hey). These two molecules represent a core protein building block and a core metabolite, respectively. The former has been used to display unique sub-molecular in situ STM resolution [152]. The latter shows a unique dual surface dynamics pattern that could be followed both by single-molecule in situ STM and by high-resolution capacitive voltammetry. [Pg.100]

Fig. 7.1 Protein building blocks. (A) The polypeptide chain, with a closeup showing the chemical form of the backbone , to which the side chains R , R +i,..., are attached. The (C=0) and (N-H) groups are linked by the peptide bond, which has a partial double bond character, making the (C=0)-(N-H) peptide group stiff and approximately planar. The torsion angles tj) and tfr, around single bonds, are soft. (B) The side chains R , R +i,..., can be any of the twenty common amino acid side chains, shown here labeled by their conventionial three-letter abbreviations (see also text). The horizontal axis corresponds roughly to the polarity of the sidechain the vertical axis corresponds to size. Reprinted from Thomas Simonson (2003) Electrostatics and dynamics of proteins. Reports on progresses in physics, vol 66, pp 737-787 with kind permission of lOP Pubhshing... Fig. 7.1 Protein building blocks. (A) The polypeptide chain, with a closeup showing the chemical form of the backbone , to which the side chains R , R +i,..., are attached. The (C=0) and (N-H) groups are linked by the peptide bond, which has a partial double bond character, making the (C=0)-(N-H) peptide group stiff and approximately planar. The torsion angles tj) and tfr, around single bonds, are soft. (B) The side chains R , R +i,..., can be any of the twenty common amino acid side chains, shown here labeled by their conventionial three-letter abbreviations (see also text). The horizontal axis corresponds roughly to the polarity of the sidechain the vertical axis corresponds to size. Reprinted from Thomas Simonson (2003) Electrostatics and dynamics of proteins. Reports on progresses in physics, vol 66, pp 737-787 with kind permission of lOP Pubhshing...
Hydrogenation reactions that are efficiently controlled by chiral Rh-phosphine catalysts involve those carbon-carbon double bonds substituted with carboxylic and amide groups. They are precursors of a-amino acids, compounds that are very important protein building blocks. The best substrate is (Z)-a-acetamidocinnamic acid 10 ... [Pg.218]

Amino acids are extremely important to living systems because they form the bases of the many proteins necessary for life. There are 20 common amino acids that function as protein building blocks (Table 3.6.2). There are at least 31 additional amino acids not commonly part of natural proteins among these are some hormones and neurotransmitters (Garrett and Grisham, 1999). [Pg.115]

The hydrolysis of proteins affords a mixture of about 20 a-amino acids. With the single exception of glycine, these amino acids contain an asymmetrically substituted a-carbon atom and, hence, are optically active. Moreover, in terms of absolute configuration, these protein building blocks share a... [Pg.86]

We pointed out at the beginning of the chapter that all enantiomeric purity must ultimately derive from nature. We have almost come full circle the reactions we have just been looking at use one of nature s protein building blocks, L-proline, directly as a catalyst. Even more intriguingly, the reaction just above, which forms a ketodiol, is extremely reminiscent of the aldol reactions which nature uses to build carbohydrates, as you will see in the next chapter. [Pg.1132]

The indole ring system, which occurs in several important natural products, is usually biosynthesized from the amino acid tryptophan, one of the protein building blocks. Indole itself and its 3-methyl derivative, skatole, are formed during protein decay. [Pg.403]


See other pages where Protein building blocks is mentioned: [Pg.13]    [Pg.474]    [Pg.547]    [Pg.55]    [Pg.651]    [Pg.126]    [Pg.1118]    [Pg.453]    [Pg.12]    [Pg.9]    [Pg.102]    [Pg.20]    [Pg.440]    [Pg.285]    [Pg.26]    [Pg.3]    [Pg.7]    [Pg.28]    [Pg.538]    [Pg.60]    [Pg.247]    [Pg.58]    [Pg.470]    [Pg.1225]    [Pg.1563]    [Pg.5]    [Pg.5]    [Pg.367]   
See also in sourсe #XX -- [ Pg.37 , Pg.41 ]

See also in sourсe #XX -- [ Pg.9 ]




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