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Concept 5.4: Proteins have many structures, resulting in a wide range of functions • Proteins account for more than 50% of the dry mass of most cells • Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Table 5-1 • Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions • Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-16 Substrate (sucrose) Glucose OH Fructose HO Enzyme (sucrase) H2O Polypeptides • Polypeptides are polymers built from the same set of 20 amino acids • A protein consists of one or more polypeptides Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Amino Acid Monomers • Amino acids are organic molecules with carboxyl and amino groups • Amino acids differ in their properties due to differing side chains, called R groups Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-UN1 carbon Amino group Carboxyl group Fig. 5-17 Nonpolar Glycine (Gly or G) Valine (Val or V) Alanine (Ala or A) Methionine (Met or M) Leucine (Leu or L) Trypotphan (Trp or W) Phenylalanine (Phe or F) Isoleucine (Ile or I) Proline (Pro or P) Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine Glutamine (Asn or N) (Gln or Q) Electrically charged Acidic Aspartic acid Glutamic acid (Glu or E) (Asp or D) Basic Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H) Amino Acid Polymers • Amino acids are linked by peptide bonds • A polypeptide is a polymer of amino acids • Polypeptides range in length from a few to more than a thousand monomers • Each polypeptide has a unique linear sequence of amino acids Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-18 Peptide bond (a) Side chains Peptide bond Backbone (b) Amino end (N-terminus) Carboxyl end (C-terminus) Protein Structure and Function • A functional protein consists of one or more polypeptides twisted, folded, and coiled into a unique shape Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-19 Groove Groove (a) A ribbon model of lysozyme (b) A space-filling model of lysozyme • The sequence of amino acids determines a protein’s three-dimensional structure • A protein’s structure determines its function Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-20 Antibody protein Protein from flu virus Four Levels of Protein Structure • The primary structure of a protein is its unique sequence of amino acids • Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain • Tertiary structure is determined by interactions among various side chains (R groups) • Quaternary structure results when a protein consists of multiple polypeptide chains Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings • Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word • Primary structure is determined by inherited genetic information Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-21a Primary Structure 1 +H 5 3N Amino end 10 Amino acid subunits 15 20 25 • The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone • Typical secondary structures are a coil called an helix and a folded structure called a pleated sheet Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-21c Secondary Structure pleated sheet Examples of amino acid subunits helix • Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents • These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions • Strong covalent bonds called disulfide bridges may reinforce the protein’s structure Animation: Tertiary Protein Structure Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-21f Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond • Quaternary structure results when two or more polypeptide chains form one macromolecule • Collagen is a fibrous protein consisting of three polypeptides coiled like a rope • Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-21g Polypeptide chain Chains Iron Heme Chains Hemoglobin Collagen Sickle-Cell Disease: A Change in Primary Structure • A slight change in primary structure can affect a protein’s structure and ability to function • Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-22 Normal hemoglobin Primary structure Sickle-cell hemoglobin Primary structure Val His Leu Thr Pro Glu Glu 1 2 3 Secondary and tertiary structures 4 5 6 7 subunit Secondary and tertiary structures Val His Leu Thr Pro Val Glu 1 2 3 Exposed hydrophobic region Quaternary structure Normal hemoglobin (top view) Quaternary structure Sickle-cell hemoglobin Function Molecules do not associate with one another; each carries oxygen. Function Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. 10 µm Red blood cell shape Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. 4 5 6 7 subunit 10 µm Red blood cell shape Fibers of abnormal hemoglobin deform red blood cell into sickle shape. What Determines Protein Structure? • In addition to primary structure, physical and chemical conditions can affect structure • Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel • This loss of a protein’s native structure is called denaturation • A denatured protein is biologically inactive Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-23 Denaturation Normal protein Renaturation Denatured protein Protein Questions • What type of bond joins two amino acids? – Peptide, covalent • Name the 2 common secondary structures of a protein. – helix and pleated sheet • List the possible types of interactions at the tertiary level of a protein. – Hydrophobic / Hydrophillic, Van der Waals, Hydrogen bonding, Disulfide bridge, ionic bonding Concept 5.5: Nucleic acids store and transmit hereditary information • The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene • Genes are made of DNA, a nucleic acid Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings The Roles of Nucleic Acids • There are two types of nucleic acids: – Deoxyribonucleic acid (DNA) – Ribonucleic acid (RNA) • DNA provides directions for its own replication • DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis • Protein synthesis occurs in ribosomes Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-26-3 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore Ribosome 3 Synthesis of protein Polypeptide Amino acids The Structure of Nucleic Acids • Nucleic acids are polymers called polynucleotides • Each polynucleotide is made of monomers called nucleotides • Each nucleotide consists of a nitrogenous base, a pentose sugar, and a phosphate group • The portion of a nucleotide without the phosphate group is called a nucleoside Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-27 5 end Nitrogenous bases Pyrimidines 5 C 3 C Nucleoside Nitrogenous base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Phosphate group 5 C Sugar (pentose) Adenine (A) Guanine (G) (b) Nucleotide 3 C Sugars 3 end (a) Polynucleotide, or nucleic acid Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars Nucleotide Monomers • Nucleoside = nitrogenous base + sugar • There are two families of nitrogenous bases: – Pyrimidines (cytosine, thymine, and uracil) have a single six-membered ring – Purines (adenine and guanine) have a sixmembered ring fused to a five-membered ring • In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose • Nucleotide = nucleoside + phosphate group Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Nucleotide Polymers • Nucleotide polymers are linked together to build a polynucleotide • Adjacent nucleotides are joined by covalent bonds that form between the –OH group on the 3 carbon of one nucleotide and the phosphate on the 5 carbon on the next • These links create a backbone of sugarphosphate units with nitrogenous bases as appendages • The sequence of bases along a DNA or mRNA polymer is unique for each gene Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings The DNA Double Helix • A DNA molecule has two polynucleotides spiraling around an imaginary axis, forming a double helix • In the DNA double helix, the two backbones run in opposite 5 → 3 directions from each other, an arrangement referred to as antiparallel • One DNA molecule includes many genes • The nitrogenous bases in DNA pair up and form hydrogen bonds: adenine (A) always with thymine (T), and guanine (G) always with cytosine (C) Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings Fig. 5-28 5' end 3' end Sugar-phosphate backbones Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 3' end 5' end New strands 5' end 3' end 5' end 3' end Nucleic Acid Questions • What are the “parts” of a nucleotide? – Sugar, phosphate and nitrogen base • Name the purines and pyrimidines. – Purine – adenine and guanine – Pyrimidine – thymine, cytosine and uracil • What two molecules make up the uprights of DNA? – Nitrogen bases held together by hydrogen bonds