Bio 101 Exam 2 Slide Vocab

Isomers

Molecules with that came chemical formula but atoms are arranged differently

Structural Isomers

Differ in how atoms are joined together

Cis-Trans Isomers

Different orientation around a double bond

Optical Isomers

Occur when C atom has four different groups attached to it (An asymmetric carbon)

Macromolecule

Polymer containing thousands or more atoms

Functional Groups

Small groups of atoms that have specific chemical properties

OH

Hydroxyl group

COOH

Carboxyl group

NH2

Amino group

PO4²-

Phosphate group

Condensation reactions

Form polymers required and H2O molecule removed

Hydrolysis reaction

Break down polymers into monomers, energy released and H2O consumed

Shape

Protein function based on:

Enzyme

Protein that catalyzes reactions

Amino Acid

Monomers of proteins that have carboxyl and amino group

Polypeptide Chain

Single, unbranched chains of amino acids that fold into specific 3D shapes as defined by amino acid sequence

Side Chain/ R-Group

Variable group that also contains functional groups

20

How many standard amino acids?

Peptide Linkages/Bonds

Covalent bond formed from a condensation reaction that joins amino acids

They must fold

What must polypeptides do to form proteins

Primary structure

Sequence of amino acids that determines how a protein is folded

Secondary Structure

Localized regularities of structure that have spatial patterns in different regions of the polypeptide chain - coils and sheets

Alpha Helix

Right handed coil resulting from hydrogen bonding between N-H and C=O groups

Beta Pleated Sheets

Two or more polypeptide chains aligned, hydrogen bonds form between chains

Tertiary Structure

Folding results in specific 3D shape of on polypeptide, determined by interactions between R-Groups

Quaternary Structure

Overall protein shape due to interaction between multiple polypeptides that make up the functional protein

Denatured Protein

Protein whose secondary and tertiary structure has been broken down

High temperature, pH changes, high concentration of polar molecules, and nonpolar substances

What affects secondary and tertiary structures and denatures them?

The primary structure

What specifies how a protein folds inot a functional 3D structure?

Yes, changes what it looks like and changes the function

Would changing an amino acid affect the protein’s tertiary structure?

Chaperones

Protect 3D structure of other proteins, prevent inappropriate reactions

Carbohydrate formula

(C1,H2,O1)n

Monosaccharides

Simple sugars

Disaccharides

Two simple sugars linked by covalent bonds

Oligosaccharides

3-20 monosaccharides

Polysaccharides

hundreds or thousands of monosaccharides

Glyceraldehyde

Three-carbon sugar, smallest monosaccharide, exists only as a straight chain

Pentoses

Sugars with 5 carbons, Ribose and Deoxyribose

Ribose has a hydroxyl group where Deoxyribose only has a hydrogen

What is different between Ribose and Deoxyribose?

Hexoses

Sugars with 6 carbons

Glucose

Monosaccharide, used by all cells as energy source, straight or ring form

Glycosidic Linkage

Covalent bond formed from a condensation reaction that joins monosaccharides

Polysaccharides

large polymers of monosaccharides

Cellulose

Very stable, good for structural components, unbranched

Starch

Glucose storage in plants, branched

Glycogen

Glucose storage in animals, highly branched

Lipids

Non-polar hydrocarbons that are insoluble in water

Fatty Acid

Non-polar hydrocarbon chain with a polar carboxyl group

Ester Linkage

How carboxyls bond with hydroxyls of glycerol

Triglycerides

Three fatty acids plus a glycerol

Saturated Fatty Acid

No double bonds between carbons, lots of hydrogens

Unsaturated Fatty Acids

One or more double bonds i carbon chain, kinks and less carbons

Phospholipids

Fatty acids bound to glycerol, a phosphate group replaces one fatty acid

Amphipathic

2 opposing chemical properties in one molecule

Bilayer

In water, phospholipids line up with hydrophobic tails together and phosphate heads facing outwards

Nucleic Acids

Specialized fo storage, transmission, and use of genetic information

Nucleotides

Monomers of nucleic acids

Nucleoside

Pentose sugar + nitrogenous base

Purines

Adenine and Guanine - double ring structure

Pyrimidines

Cytosine,Thymine, and Uracil - 6 membered single ring

Phosphodiester Linkages

Bond between two nucleotides

Complementary base pairing

Purines pair with pyrimidines via hydrogen bonds, A-T, G-C

Double Helix

Two strands of DNA, form a ladder that twists

Why is DNA important?

Passed down generation to generation and codes for proteins

Genome

All the DNA in an organism

Replication

Duplication of genetic material

Transcription and Translation

Processes that lead to protein formation

ATP

Energy transfer in biochemical reactions

GTP

Energy source in protein synthesis

cAMP

Essential to action of hormones and transmission of info in the nervous system

Spontaneous Generation

Creating life from inanimate objects/nature

Chemical Evolution

Conditions of primitive Earth led to formation of simple molecules, which led to formation of life forms

Catalysts

Proteins called enzymes that speed up reactions

Ribozymes

Catalytic RNAs that speed up reactions involving their own nucleotides

Membrane

Barrier separating internal contents of cell from external environment, allows cell to maintain chemical composition different from outside

Lipid Bilayer

Fatty acids form this in water

Protocells

Stepping stones for origin of cells

High surface area to volume ratio

Why are cells so small?

Magnification

Increases apparent size

Resolution

Clarity of magnified object, minimum distance two objects can. be apart and still be seen as two objects

Scanning electron microscopes

Can see details on cell surface

Transmission electron microscope

Can see internal cell structures

A cell membrane, DNA, cytoplasm, and ribosomes

All cells have:

Cell membrane, nucleoid, cytoplasm, and ribosomes

All Prokaryotic cells have:

Nucleoid

Region where DNA is located in prokaryotic cells

Outer Membrane

Additional phospholipid membrane found outside the peptidoglycan layer

Capsule

Slimy layer of polysaccharides, protects prokaryotic cells

Pili

Hairlike structures projecting from cell surface, help bacteria adhere to other cells

Cytoskeleton

Protein filaments important for cell division, movement, and maintaining cell shape

Ribosomes

Site of protein synthesis

Endomembrane System

Interconnected system of membrane enclosed compartments

Cell membrane, nuclear envelope, ER, golgi apparatus, and lysosomes

What are the parts of the endomembrane system?

Vesicles

Tiny membrane surrounded structures that shuttle substances between various components

Nucleolus

Within nucleus, assembly of ribosomes

Nuclear envelope

Double membrane surrounding nucleus and has pores to control movement of molecules in and out of nucleus

ER

Network of membranes in cytoplasm with large surface area

Rough ER

Has ribosomes attached, newly made proteins enter lumen and are modified, folded, and transported elsewhere

Smooth ER

No ribosomes, Chemically modifies small molecules such as drugs, site of glycogen degradation in animal cells, synthesis of lipids, and stored calcium ions

Golgi Apparatus

Flattened sacs (cisternae) and small vesicles, recieves proteins from RER and modifies them further, concentrates, packages, and sorts proteins, and synthesizes polysaccharides for cell wall in plant cells

Phagocytosis

Process of ingesting particles or other cells into a cell