Chapter 2 Structure and Function of Nucleic Acids. Introduction
The two strands of the double-helical molecule, each of which possesses a polarity, are antiparallel; ie, one strand runs in the 5’to 3’ direction and the other in the 3’ to 5’direction. The two strands, in which opposing bases are held together by hydrogen bonds, wind around a central axis in the form of a double helix. The genetic information resides in the sequence of nucleotides on one strand, the template strand. This is the strand of DNA that is copied during nucleic acid synthesis.
Three kinds of DNA double-helix
Circled DNA compounds.
Figure 4-8. The denaturation and renaturation of double-stranded DNA molecules.
Curve of DNA melting double-stranded DNA molecules.
RNA is a polymer of purine and pyrimidine ribonucleotides linked together by 3’, 5’-phosphodiester bridges analogous to those in DNA. Although sharing many features with DNA, RNA possesses several specific differences.
(Only on some caps)
7-methylguanosine triphosphate cap
Figure 4-18. Structure of the 5′ methylated cap of eukaryotic mRNA.
Figure 4-19. Overview of RNA processing in eukaryotes using β-globin gene as an example. The β-globin gene contains three protein-coding exons (red) and two intervening noncoding introns (blue). The introns interrupt the protein-coding sequence between the codons for amino acids 31 and 32 and 105 and 106. Transcription of this and many other genes starts slightly upstream of the 5′ exon and extends downstream of the 3′ exon, resulting in noncoding regions (gray) at the ends of the primary transcript. These regions, referred to as untranslated regions (UTRs), are retained during processing. The 5′ 7-methylguanylate cap (m7Gppp; green dot) is added during formation of the primary RNA transcript, which extends beyond the poly(A) site. After cleavage at the poly(A) site and addition of multiple A residues to the 3′ end, splicing removes the introns and joins the exons. The small numbers refer to positions in the 147-aa sequence of β-globin.
Figure 4-30. Recognition of a tRNA by aminoacyl synthetases. Aspartyl-tRNA synthetase (AspRS) is a class II enzyme, and arginyl-tRNA synthetase (ArgRS) is a class I enzyme.
Figure 4-26. Structure of tRNAs. Aspartyl-tRNA synthetase (AspRS) is a class II enzyme, and arginyl-tRNA synthetase (ArgRS) is a class I enzyme.
Figure 6-11. Aspartyl-tRNA synthetase (AspRS) is a class II enzyme, and arginyl-tRNA synthetase (ArgRS) is a class I enzyme.Amino acid activation. The two-step process in which an amino acid (with its side chain denoted by R) is activated for protein synthesis by an aminoacyl-tRNA synthetase enzyme is shown. As indicated, the energy of ATP hydrolysis is used to attach each amino acid to its tRNA molecule in a high-energy linkage. The amino acid is first activated through the linkage of its carboxyl group directly to an AMP moiety, forming an adenylated amino acid;the linkage of the AMP, normally an unfavorable reaction, is driven by the hydrolysis of the ATP molecule that donates the AMP. Without leaving the synthetase enzyme, the AMP-linked carboxyl group on the amino acid is then transferred to a hydroxyl group on the sugar at the 3' end of the tRNA molecule. This transfer joins the amino acid by an activated ester linkage to the tRNA and forms the final aminoacyl-tRNA molecule. The synthetase enzyme is not shown in these diagrams.
Figure 4-29. Aminoacylation of tRNA. Amino acids are covalently linked to tRNAs by aminoacyl-tRNA synthetases.
Figure 4-22. Assigning codons using synthetic mRNAs containing a single ribonucleotide. Addition of such a synthetic mRNA to a bacterial extract that contained all the components necessary for protein synthesis except mRNA resulted in synthesis of polypeptides composed of a single type of amino acid as indicated.
A ribosome is a cytoplasmic nucleoprotein structure that acts as the machinery for the synthesis of proteins from the mRNA templates. On the ribosomes, the mRNA and tRNA molecules interact to translate into a specific protein molecule information transcribed from the gene.
Figure 4-32. The general structure of ribosomes in prokaryotes and eukaryotes.
Figure 4-33. Two-dimensional map of the secondary structure of the small (16S) rRNA from bacteria, showing the location of base-paired stems and loops. In general, the length and position of the stem-loops are very similar in all species, although the exact sequence varies from species to species. The most highly conserved regions are represented as red lines, and the numbered stem-loops unique to prokaryotes are preceded by a P. Eukaryotic small (18S) rRNAs exhibit a generally similar pattern of stem-loops, although, as with prokaryotes, a few are unique.
Figure 4-20. The three roles of RNA in protein synthesis. of the small (16S) rRNA from bacteria, showing the location of base-paired stems and loops.
Figure 4-25. Translation of nucleic acid sequences in mRNA into amino acid sequences in proteins requires a two-step decoding process. First, an aminoacyl-tRNA synthetase couples a specific amino acid to its corresponding tRNA. Second,a three-base sequence in the tRNA (the anticodon) base-pairs with a codon in the mRNA specifying the attached amino acid. If an error occurs in either step, the wrong amino acid may be incorporated into a polypeptide chain.
Figure 6-17. into amino acid sequences in proteins requires a two-step decoding process.The genetic code. The standard one-letter abbreviation for each amino acid is presented below its three-letter abbreviation. Codons are written with the 5'-terminal nucleotide on the left. Note that most amino acids are represented by more than one codon and that variation is common at the third nucleotide (see also Figure 3-16).
Figure 4-35. Two types of methionine tRNA are found in all cells. One, designated tRNAiMet, is used exclusively to start protein chains, and the other, designated tRNAMet, delivers methionine to internal sites in a growing protein chain. In bacteria, a formyl group (CHO) is added to methionyl-tRNAiMet, forming fMet-tRNAiMet
1. The element that could be used in nucleic acid quantitation is ( )
2. The basic unit composition of nucleic acid is ( ) quantitation is ( )
A. Ribose and deoxyribose
B. phosphoric acid and pentaglucose
C. Pentaglucose and basic group
E. phosphoric acid，pentose and basic group
3 quantitation is ( )．脱氧核糖核苷酸彻底水解，生成的产物的产物是( )
4 quantitation is ( )．在核酸分子中核苷酸之间的连接方式是( )
C. 2’,5’ －磷酸二酯键
6. about ( )含有稀有碱基比例较多的核酸是( )
7. about ( )核酸分子中储存、传递遗传信息的关键部分是( )
8 about ( )．DNA分子碱基含量关系哪种是错误的？
9. ATP about ( )的生理功能不包括( )
10. about ( )下列哪种核酸的二级结构具有”三叶草”型?
11. about ( )关于mRNA的论述不正确的是( )
13. DNA about ( )变性是指( )
14. DNA Tm about ( )值较高是由于下列哪组核苷酸含量较高所致?
15. Where does DNA reside in? about ( )
A. Golgi's body
B. rough endoplasmic reticulum
16. about ( )含有腺苷酸的辅酶有( )
17. about ( )关于tRNA的论述不正确的是( )
18. about ( )维持DNA双螺旋结构的稳定因素包括( )
19. DNA about ( )变性的实质是( )
20. What does the T about ( )m refer to about DNA?
A. optimum temperature
B. hydrolytic temperature
C. Renaturation temperature
D. melting temperature
E. denaturation temperature
Thank you! about ( )