Prologue to Organic chemistry.


48 views
Uploaded on:
Category: Medical / Health
Description
Natural chemistry gives a crucial comprehension of life. ... History of Biochemistry. Arabic science - enormously impacted by right on time Greek exploratory ...
Transcripts
Slide 1

Prologue to Biochemistry Connie Giroux BME 602 SDSMT/USD Spring 2007

Slide 2

Overview of Topics History of Biochemistry Formation of Biomolecules Dynamic Functions of Biomolecules: amino acids peptides proteins enzymes carbohydrates lipids Cellular Metabolism

Slide 3

Biochemistry "The science of the living cell." Describes the procedures of life at the level of atoms. Has segments of both science and science. Need a comprehension of the natural capacity of cell particles. Need learning of substance structures of the taking an interest atoms.

Slide 4

Why Study Biochemistry? Organic chemistry gives a key comprehension of life. Helps with our comprehension of drug, wellbeing, and nourishment. Biochemical disclosures will propel biotechnology-the use of organic cells, cell parts, and natural procedures to in fact helpful operations.

Slide 5

History of Biochemistry Early studies in science had firm roots in theory and religion. Thinks about focused on treatment of ailment and fulfillment of good wellbeing. Fourth century B.C.- Chinese trusted people contained five components: water, fire, wood, metal, and earth. Early Greeks-clarified the body regarding cosmological speculations and utilized eating routine for the treatment of ailment.

Slide 6

History of Biochemistry Arabic science - extraordinarily impacted by early Greek exploratory writing and propelled Greek pharmaceutical formulas by deciding and characterizing the quality and concoction nature of normal medications. Europe - Paracelsus (1493-1541 A.D.) had progressive thoughts regarding pharmaceutical and science. 17 th and 18 th century researcher - had a more sub-atomic way to deal with the investigation of organic material and procedures. 19 th century – utilized vitalism to portray any natural procedure that couldn\'t be comprehended in concoction terms.

Slide 7

Modern Biochemistry Two unmistakable ways prompted current comprehension: 1 st way - physical sciences used to underscore the basic qualities of biomolecules. Essential laws of material science and science are utilized to clarify the procedures of living cells. 20 th century – Linus Pauling utilized X-beam crystallography to study protein structures. 2 nd way – the investigation of cell association and capacity by scholars, physiologists, and geneticists. 1952 – two ways met when twofold helix structure for DNA was proposed by James Watson and Francis Crick.

Slide 8

Boyer, 1999

Slide 9

Elements in Biomolecules Over 100 concoction components – just around 28 happen normally in plants and creatures. Three classes for components found in natural material: 1: Elements found in mass shape and are key forever: C, H, O, N, P, S (make up 92% of the dry weight of living things). 2: Elements found in follow amounts and likely vital forever: Ca, Mn, Fe, I. 3: Trace components that might be crucial forever: As, Br, Mo.

Slide 10

Elements in Biomolecules fluctuate in their concoction structure and reactivity in light of the compound components that are joined with them.

Slide 11

Biological Macromolecules Three noteworthy classes of common macromolecules found in organic cells: nucleic acids, proteins, and polysaccharides. All macromolecules are polymers.

Slide 12

Biological Macromolecules Nucleic acids – heteropolymers made out of nucleotides. Proteins – heteropolymers delivered by consolidating amino acids. Polysaccharides – made out of numerous saccharide atoms.

Slide 13

Supramolecular Assemblies Organized bunches of macromolecules. Cell films: edifices of proteins and lipids. Chromatin: buildings of DNA and proteins. Ribosomes: edifices of RNA and proteins. Infections: single DNA or RNA atom contained in a protein bundle.

Slide 14

Cells Fundamental unit of life. Living cells contain mixes speaking to every one of the three conditions of matter (gasses, fluids, and solids). Three fundamental groupings of life forms: Eukaryotes (particular film encased core and very much characterized inside compartments) Prokaryotes (straightforward, unicellular creatures with no unmistakable core or inward cell compartments) Archaebacteria (flourish in compelling situations)

Slide 15

Flow of Biological Information DNA Signal transduction – the nearness of a particle outside of the phone which transfers a charge to an inside cell segment.

Slide 16

Boyer, 1999

Slide 17

DNA and RNA Structural and practical components. Biosynthesis of DNA and RNA. Interpretation of RNA. Recombinant DNA innovation and their applications.

Slide 18

Biomolecules in Water Typical cell contains 70 to 85% water. Water can be utilized as a dissolvable or as a reactant atom. Hydrolysis – breaking of a compound bond by water. All biomolecules are not dissolvable in water. Life forms make films from water insoluble atoms.

Slide 19

Amino Acids Amino corrosive – any natural particle with no less than one carboxyl gathering (natural corrosive) and no less than one amino gathering (natural base). 20 amino acids are hereditarily coded for joining into proteins. Involved carbon focus ( α - carbon) encompassed by a hydrogen, a carboxyl gathering, an amino gathering, and a R side chain. Side chain decides the exceptional compound and organic reactivity of every amino corrosive.

Slide 20

Boyer, 1999

Slide 21

Peptides Peptide bond – carboxyl gathering on one amino corrosive bonds with the amino gathering of the other amino corrosive through buildup (loss of a water particle). Peptides – contain 2 to 10 amino acids. Polypeptides – contain 10 to 100 amino acids. Proteins – contain more than 100 amino acids.

Slide 22

Proteins Provide mechanical backing to cells and living beings. Utilized as a natural impetus (catalyst). Used to transport littler biomolecules and store supplements. Are useful segments of the contractile arrangement of skeletal muscle. Utilized as a guard instrument (antibodies). Controls cell and physiological movement (hormones). Intercedes transmission of nerve driving forces and hormone signals (receptor proteins).

Slide 23

Four Levels of Protein Structure Primary Structure: the grouping (request) of amino corrosive buildups in a protein held together by covalent peptide bonds. Auxiliary Structure: confined districts of the essential arrangement collapsed into customary, rehashing structures ( α - helix or β - sheet). Tertiary Structure: auxiliary basic components associate and pack into a minimal globular unit. Quarternary Structure: relationship of two or more polypeptide chains to frame a multi-subunit protein atom.

Slide 24

Boyer, 1999

Slide 25

Enzymes Biological impetuses. Michaelis-Menten Equation – numerical relationship between the rate of a compound catalyzed response and the convergence of a protein and substrate. Lineweaver-Burk Equation – corresponding of the Michaelis-Menten condition; Lineweaver-Burk plot used to decide constants for chemical catalyzed responses and assesses the restraint of compound responses.

Slide 26

ν 0 = V max [S]/{K M + [S]} Boyer, 1999

Slide 27

1/ν 0 = {K M/V max } {1/[S]} + 1/V max Boyer, 1999

Slide 28

Enzymes Coenzymes – natural or organometallic particle that helps a protein. Allosteric proteins – transmit messages, through conformational changes, between restricting destinations that are spatially unmistakable. Isoenzymes – various types of a compound that have comparative however not indistinguishable amino corrosive groupings and response qualities.

Slide 29

Carbohydrates Used in vitality digestion system (glucose). Performs auxiliary capacities (plant cell dividers and exoskeleton shells). Ribose and deoxyribose (parts of nucleic acids) serve a concoction basic part in RNA and DNA and are polar locales for reactant forms (RNA). Serves as a marker for sub-atomic acknowledgment by different biomolecules.

Slide 30

Lipids Distinctive trademark is their solvency conduct. Hydrophobic nature so more dissolvable in non-polar solvents (diethyl ether, methanol, hexane) than in water. Characterized by their physical conduct as opposed to their compound structure. Lipid families: unsaturated fats, triacylglycerols, polar lipids, steriods. Layers – fluid–mosaic model, dynamic and aloof transport, Na + - K + ATPase pump, and particle specific channels.

Slide 31

Cellular Metabolism Catabolism is partitioned into three noteworthy stages: 1: Breakdown of macromolecules (proteins, fats, polysaccharides) – planning stage for the following level of responses. 2: Amino acids, unsaturated fats, and monosaccharides are oxidized to a typical metabolite, acetyl CoA. 3: Acetyl CoA enters citrus extract cycle and is oxidized to CO 2 , the finished result of high-impact carbon digestion system.

Slide 32

Cellular Metabolism Anabolism is isolated into three phases: 1: Monosaccharide and polysaccharide combinations may start with CO 2 , oxaloacetate, pyruvate, or lactate. 2: Amino acids for protein blend are shaped from acetyl CoA and by the amination of pyruvate and α - keto acids from the citrus extract cycle. 3: Triacylglycerols are built utilizing unsaturated fats blended from acetyl CoA.

Slide 33

Boyer, 1999

Slide 34

Fox, 2006

Slide 35

Metabolism of Carbohydrates Glycolysis – comprises of ten catalyst catalyzed responses that start with a hexose substrate and split into two particles of pyruvate, a α - keto corrosive. Two phases of glycolysis: 1: Investment stage – glucose (a six-carbon substrate) is part into two particles of a three-carbon metabolite; two ATP atoms are expended for every glucose atom that enters pathway.

Slide 36

Metabolism of Carbohydrates 2: Dividend stage – every three-carbon metabolite is changed into another three-carbon metabolite (pyruvate). Four ATP particles and two NADH atoms created in stage 2. General yield: two ATP and two NADH.

Slide 37

Figure 5.2 Glycolysis Fox, 2006

Slide 38

Metabolism of Carbohydrates Lactate fermen

Recommended
View more...