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By Harvey Lodish, Arnold Berk, Paul Matsudaira, Chris A. Kaiser, Monty Krieger, Matthew P. Scott, Lawrence Zipursky, James Darnell

Molecular phone Biology sticks out from its friends during this path in that it offers a transparent creation to the innovations and experiments of scientists prior and current, not only an “encyclopedia” of information.  This experimental emphasis, including an outstanding pedagogical framework within the chapters, presents the clearest, so much state of the art textual content on hand.

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Miles from A. A. , 2000, Biophys J. ] T he life of a cell depends on thousands of chemical interactions and reactions exquisitely coordinated with one another in time and space and under the influence of the cell’s genetic instructions and its environment. How does a cell extract critical nutrients and information from its environment? How does a cell convert the energy stored in nutrients into work (movement, synthesis of critical components)? How does a cell transform nutrients into the fundamental structures required for its survival (cell wall, nucleus, nucleic acids, proteins, cytoskeleton)?

Because the C␣ in all amino acids, except glycine, is asymmetric, these molecules have two mirrorimage forms, designated L and D. Although the chemical properties of such optical isomers are identical, their biological activities are distinct. Only L amino acids are found in proteins. COO− NH3+ Cα H 39 NH3+ Cα H R D isomer R L isomer HYDROPHOBIC AMINO ACIDS COO؊ ؉H N 3 C COO؊ ؉H N 3 H C CH3 COO؊ H ؉H N 3 C H H C CH3 CH H3C COO؊ CH3 ؉H N 3 CH2 H3C CH3 C COO؊ ؉H N 3 H C CH2 CH2 CH CH2 CH3 H COO؊ ؉H N 3 C COO؊ ؉H H 3N C CH2 Valine (Val or V) Isoleucine (Ile or I) Methionine (Met or M) Acidic amino acids ؉H N 3 C COO؊ ؉H N 3 H C ؉H N 3 COO؊ ؉H N 3 H C CH2 CH2 C NH CH2 CH2 C H N؉ H NH2؉ C C ؉H N 3 Histidine (His or H) C H COO؊ ؉H 3N C H H C OH CH2 OH CH3 Serine (Ser or S) Threonine (Thr or T) COO؊ H ؉H N 3 CH2 Arginine (Arg or R) Tryptophan (Trp or W) COO؊ COO؊ ؉H N 3 ؊ COO H 2N C H COO؊ ؉H 3N SPECIAL AMINO ACIDS COO؊ ؉H 3N C CH2 H COO؊ ؉H N 3 C H H2C SH Cysteine (Cys or C) H COO؊ H C ؉H N CH2 2 Glycine (Gly or G) CH2 Proline (Pro or P) C H CH2 CH2 C CH2 O C H 2N Glutamate (Glu or E) CH NH Polar amino acids with uncharged R groups CH2 NH2 Lysine (Lys or K) H Aspartate (Asp or D) CH NH CH2 Tyrosine (Tyr or Y) COO CH2 NH3؉ Phenylalanine (Phe or F) ؊ CH2 CH2 C H OH CH2 H CH2 C C COO؊ Basic amino acids COO؊ 3N S Leucine (Leu or L) HYDROPHILIC AMINO ACIDS ؉H H CH2 CH3 Alanine (Ala or A) COO؊ Asparagine (Asn or N) O Glutamine (Gln or Q) ▲ FIGURE 2-13 The 20 common amino acids used to build proteins.

Bottom) In contrast, phospholipid monomers noncovalently assemble into bilayer structure, which forms the basis of all cellular membranes (Chapter 5). 38 CHAPTER 2 • Chemical Foundations are linear polymers containing hundreds to millions of nucleotides linked by phosphodiester bonds. Polysaccharides are linear or branched polymers of monosaccharides (sugars) such as glucose linked by glycosidic bonds. A similar approach is used to form various large structures in which the repeating components associate by noncovalent interactions.

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