B. Alberts, A. Johnson, J. Lewis и др. - Molecular Biology of The Cell (6th edition) (1120996), страница 42
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New Haven, CT: Yale University Press.Martijn J & Ettma TJG (2013) From archaeon to eukaryote: theevolutionary dark ages of the eukaryotic cell. Biochem. Soc. Trans.41, 451–457.Mulkidjanian AY, Bychkov AY, Dibrova DV et al. (2012) Open questionson the origin of life at anoxic geothermal fields. Orig. Life Evol.Biosph. 42, 507–516.Zimmer C (2009) On the origin of eukaryotes. Science 325, 665–668.109CHAPTERProteinsWhen we look at a cell through a microscope or analyze its electrical or biochemical activity, we are, in essence, observing proteins. Proteins constitute mostof a cell’s dry mass. They are not only the cell’s building blocks; they also executethe majority of the cell’s functions.
Thus, proteins that are enzymes providethe intricate molecular surfaces inside a cell that catalyze its many chemicalreactions. Proteins embedded in the plasma membrane form channels andpumps that control the passage of small molecules into and out of the cell. Otherproteins carry messages from one cell to another, or act as signal integrators thatrelay sets of signals inward from the plasma membrane to the cell nucleus. Yetothers serve as tiny molecular machines with moving parts: kinesin, for example,propels organelles through the cytoplasm; topoisomerase can untangle knottedDNA molecules. Other specialized proteins act as antibodies, toxins, hormones,antifreeze molecules, elastic fibers, ropes, or sources of luminescence. Beforewe can hope to understand how genes work, how muscles contract, how nervesconduct electricity, how embryos develop, or how our bodies function, we mustattain a deep understanding of proteins.THE SHAPE AND STRUCTURE OF PROTEINSFrom a chemical point of view, proteins are by far the most structurally complexand functionally sophisticated molecules known.
This is perhaps not surprising, once we realize that the structure and chemistry of each protein has beendeveloped and fine-tuned over billions of years of evolutionary history. The theoretical calculations of population geneticists reveal that, over evolutionary timeperiods, a surprisingly small selective advantage is enough to cause a randomlyaltered protein sequence to spread through a population of organisms. Yet, evento experts, the remarkable versatility of proteins can seem truly amazing.In this section, we consider how the location of each amino acid in the longstring of amino acids that forms a protein determines its three-dimensional shape.Later in the chapter, we use this understanding of protein structure at the atomiclevel to describe how the precise shape of each protein molecule determines itsfunction in a cell.The Shape of a Protein Is Specified by Its Amino Acid SequenceThere are 20 different of amino acids in proteins that are coded for directly in anorganism’s DNA, each with different chemical properties.
A protein moleculeis made from a long unbranched chain of these amino acids, each linked to itsneighbor through a covalent peptide bond. Proteins are therefore also known aspolypeptides. Each type of protein has a unique sequence of amino acids, andthere are many thousands of different proteins in a cell.The repeating sequence of atoms along the core of the polypeptide chain isreferred to as the polypeptide backbone. Attached to this repetitive chain arethose portions of the amino acids that are not involved in making a peptide bondand that give each amino acid its unique properties: the 20 different amino acidside chains (Figure 3–1). Some of these side chains are nonpolar and hydrophobic3IN THIS CHAPTERTHE SHAPE AND STRUCTUREOF PROTEINSPROTEIN FUNCTION110Chapter 3: ProteinsFigure 3–1 The components of a protein.A protein consists of a polypeptidebackbone with attached side chains. Eachtype of protein differs in its sequence andnumber of amino acids; therefore, it is thesequence of the chemically different sidechains that makes each protein distinct.The two ends of a polypeptide chain arechemically different: the end carrying thefree amino group (NH3+, also written NH2)is the amino terminus, or N-terminus,and that carrying the free carboxyl group(COO–, also written COOH) is the carboxylterminus or C-terminus.
The amino acidsequence of a protein is always presentedin the N-to-C direction, reading from leftto right.OHOOCpolypeptide backboneHamino+terminusH N(N-terminus)HOCCHCH2CH2side chainsCH2NCCHHOMethionine(Met)HONCCCH2peptidebondsCHH3CSCH3HCH2ONCHHCOcarboxylterminus(C-terminus)peptide bondCH3side chainsAspartic acid(Asp)Leucine(Leu)Tyrosine(Tyr)(“water-fearing”), others are negatively or positively charged, some readily formcovalent bonds, and so on. Panel 3–1 (pp. 112–113) shows their atomic structuresand Figure 3–2 lists their abbreviations.As discussed in Chapter 2, atoms behave almost as if they were hard sphereswith a definite radius (their van der Waals radius).
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