Biochemistry 1 - biochem PDF

Title Biochemistry 1 - biochem
Author Lance William Ramirez
Course Biochemistry
Institution Far Eastern University
Pages 1
File Size 104.1 KB
File Type PDF
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Summary

biochem...


Description

AP Biology Unit 1: Biochemistry Cheat Sheet by hlewsey via cheatography.com/36676/cs/11528/

Properties of Water

Metabolism

Large Biomolecules

Polarity:

metabolic

a specific molecule that is altered

Carbohydrates 

- allows cohesion, adhesion, surface tension

pathway

in defined steps catalyzed by

High Specific Heat:

enzymes that result in a certain

- resists temp change

product

- high heat of vaporization - allows evaporative  cooling (high energy particles vaporize) Universal Solvent: - dissolves hydrophilic/  repels  hydrophobic 

catabolic

releases energy by breaking down

pathway

complex molecules

anabolic

consumes energy to build more

pathway

complex molecules

energy

the capacity to cause change or rearrange matter

Properties of Carbon

-monosacc  h  arides held by glycosidic linkages -energy storage, structure, protection Lipids -fatty acids held by ester linkages -hydrophobic, saturated/unsaturated,    hormones Nucleic Acids -nucleotides held by phosphodiester H-

tetravalenc 

4 bonds->complex molecules

Isomers

e

bonds -enable reproduction,  controls protein

hydrocarbo 

synthesis

C and H, release energy

ns

Proteins

structural

differs in covalent arrangement  of

isomer

atoms

geometric

differs in spacial arrangements

isomer

around double bonds

enantiomer

mirror image of 4 molecules

-amino acids held by peptide bonds -follow varied instructions  from DNA

attached to asymmetric carbon

Enzymes Laws of Thermodynamics 

Enzymes these macromolecules act as catalysts that

1st Law of Thermodynamics 

Functional Groups

energy can be transferred  and transfo  rmed -OH

hydroxyl

polar/hydrophilic  

-CH3

methyl

nonpolar/hydrophobic   

-COOH

carboxyl

polar/hydrophilic  

-COH

carbonyl

-NH2

amino

2nd Law of Thermodynamics 

Enzyme Activation -gene regulation=  enzymes produced when needed

polar/hydrophilic  

increases the entropy of the universe; a

-activators=cofactors (inorganic)  and

polar/hydrophilic  

process must increase entropy to be

coenzymes (organic) make up and help

spontaneous 

enzymes function

sulfhydryl

nonpolar/hydrophobic   

-PO4

phosphate

polar/hydrophilic  

Acids and Bases increases H+ in solution

Enzyme Inhibition Free Energy Gibbs free energy- ΔG=ΔH-TΔS energy in a temp/pressure  constant system that can perform work

Base

an induced fit w/substrate  in the active site

every energy transfer/transformation    

-SH

Acid

but not created or destroyed

lower activation energy barriers by forming

reduces H+ in solution (accepts H+or donates OH-)

pH

=-log[H+]

Buffer

accepts/donates H+ to stabilize pH

exergonic has a net release of free energy (-ΔG) endergonic absorbs free energy (+ΔG)

-competitive=in    hibitor molecule binds to active site to block substrate -allosteric=inhibitor molecule binds to allosteric site to cover or change shape of the active site Optimal Conditions -enzymes have optimal temp+pH -cofactors+coenzymes bind to enzyme or substrate

ATP ribose, adenine, 3 phosphate groups hydrolyzed to ADP+Pᵢ phosphorylated molecules=more reactive

By hlewsey

Published 23rd April, 2017.

cheatography.com/hlewsey/

Last updated 23rd April, 2017.

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