Chapter 1 Chemistry Flashcards by Carla Alvarez

Atom

Consist of a nucleus that has positively charged protons and neutrally charged atoms.
Electrons are located outside the nucleus and are negative.

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Molecules

Group of 2 or more atoms held by a chemical bond

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Electronegativity

Ability for atom to attract electrons

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Ionic bonds

form when one or more electrons are transferred from one atom to the other. The electroengativities are very different and one atom has a strong pull on the electrons compared to the other atom.

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Covalent bonds

Forms when electrons between atoms are SHARED

Electronegativites are similar

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Nonpolar covalent bond

Bonds when electrons are shared equally

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4 important classes of organic molecules

carbohydrates, lipids, proteins, nucleic acids

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Carbohydrates

SUGAR!! You always forget this

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Monosaccharide

Simplest for of carb.
Consists of a single sugar molecule (Fructose or Glucose)
Formula (CH2O)n

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Disaccharide

2 sugar molecules joined by a glycosidic linkage
During the process of joining a water molecule is lost
formula is C12H22O11 not C12H24O12 (due to dehydration reaction)

Glucose + fructose= sucrose
Glucose + galactose = lactose
Glucose+ glucose = maltose

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Polysaccharide

Series of connected monosaccharides (single sugar molecule)

POLYMER- has repeating units of a monosaccharide

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Starch

polymer of a-glucose

-Energy storage in PLANTS

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Glycogen

polymer of a-glucose
differs from starch by polymer branching
-Energy storage in ANIMAL CELLS

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Cellulose

Polymer of B-glucose molecules

Function: Structural molecule in the walls of PLANTS and major component of wood

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Chitin

Polymer similar of cellulose
Has B-glucose molecules has NITROGEN-CONTAINING GROUP attached to the ring.
Function: Structural molecule in walls of FUNGUS CELLS and exoskeleton of insects, antropods and mollusks

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Lipids

Insolubule in water

Soluble in nonpolar substances (ether and chloroform)

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3 Major forms of lipids?

Triglycerides, Phospholipid, Steriod

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Triglyceride

Fats and oils
3 fatty acid attached to a glycerol backbone
Fatty acids are hydroharbon (C and H with a carboxyl group -COOH)

Saturated fatty acid- all single bonds
Monosaturated fatty acid- One single bond
Polyunsaturated fatty acid- Multiple double bonds (2 or more)

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Phospholipid

Has 2 fatty acid chains, glycerol backbone, and a phosphate group (-PO3^2-) with a R group
Function: Structural foundation of cell membrane

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Steroids

backbone of 4 linked carbon rings (three 6 C and one 5C)

Ex. Cholesterol, hormones, testosterone, estrogen

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Categories of Proteins

Structural proteins- keratin (hair and horns), collegen (connective tissue), silk (spider webs)
Storage Proteins- casein in milkm ovalbumin in egg whites, zein in corn seeds
Transport proteins- Members of cells that transport materials into and out of cells
Defensive proteins- antibodies that provide protection again foreign substances that enter the bodies of animals
Enzymes- regular the rate of chemical reactions

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Amino acid

Central carbon bonded to an amino group (-NH2), a carboxyl group (-COOH) and a hydrogen atom, and R

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Proteins

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Proteins are polymers of amino acids that are covalently bonded.
Protein differs by the NUMBER and ARRANGEMENTS of amino acids

Peptide bonds

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bonds located between amino acids to make a protein

Polypeptide

A chain of amino acid and peptide bonds

Structure of Proteins

Primary, Secondary, tertiary, quarternary

Primary Structure

Describes order of amino acids

Secondary Structure

3D shape due to HYDROGEN BONDING b/w amino and carboxyl groups of aa right next to each other This makes alpha helix or beta pleated sheets

Tertiary Structure

Additional 3D shape Hydrogen bonding between R groups Ionic bonding between R groups Hydrophobic effect ( hydrophobic R groups moces away from water) Disulfide bonds ( sulfur in cysteine bonds to sulfur in another cysteins) -maintains turns of the aa chain

Quarternary Structure

When 2 or more separate peptide chains interact | Held by hydrogen bonding, interaction among R groups and disulfide bonds

DNA

Polymer of nucleotides | Consists: nitrogen base, 5 carbon sugar (deoxyribose), phosphate group

DNA nucleotides

Adenine- double ring (purine) Thymine- single ring (pyrimidine) Cytosine- single ring (pyrimidine) Guanine- double ring (purine)

Pyrimidines

single ring nitrogen bases

Purines

Double ring nitrogen bases

RNA

sugar is ribose Thymine replaced by uracil SINGLE STRANDED does not form a double helix like DNA

Catabolism

Break down of substances

Anabolism

formation of new products

Equilibrium

rate of forward equals the rate in the reverse reaction | no net production of reactants or products

Enzymes

Globular proteins that act as catalyst (activators or accelerators) for metabolic reactions

Substrate

Substance of substances which enzyme reacts

Enzymes characteristics

1. Substrate specific 2. Unchanged after a reaction and can be reused 3. Can catalyze both forward and reverse of a reaction 4. Temperature and pH affects the efficiency - above 104 becomes denatured 5. Standard suffix is "ase"

Induced fit model

There is an active site where the reactants readily interact due to shape, polarity or other characteristics. This interaction causes enzyme to change shape which places the substrate molecules into a more favorable position.

Cofactor

Non protein molecules that assist the enzyme

Holoenzyme

Union of both cofactor and enzyme

Apoenzyme

when an enzyme is part of a Holoenzyme

Coenzymes

organic cofactors that function to donate or accept component of reaction (usually electrons)

Inorganic cofactors

Metal ions, Fe2+ or Mg2+

ATP

Adenosine trophosphate | Components: Ribose, adenine and 2 phosphates?

Allosteric enzymes

have 2 binding sites - active site - and allosteric site

Allosteric activator

binds to enzyme and induces the active form

Allosteric inhibitor

binds to enzyme and induces inactive form

Feedback inhibition

end product acts as an allosteric INHIBITOR which shuts down one of the enzymes that catalyzes reaction

Competitive inhibition

Substance that mimics the substrate which inhibits the enzyme since the substance occupies the active site

Noncompetitve inhibition

Substance inhibits the enzyme by binding to the location NOT at the active site. This changes the shape of the enzyme and stops enzymatic activity

Cooperativity

enzyme becomes more sensitive to additional substrate after this substrate attaches to the active site ex. hemoglobins binding activity to o2 increases after the first o2 molecule binds to an active site

Chapter 1 Chemistry Flashcards

(55 cards)