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137 Cards in this Set

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who first introduced biochemistry

German Chemist Carl Neuberg, 1903

Biochemistry means

Chemistry of Living beings/ Chemical basis of life

biochemistry deals with

the study of biochemical reactions and processes

Branches of biochemistry

Medical


Clinical


bacterial


Plant


animal


industrial

studies the chemical basis of human body

medical biochemistry


studies clinical diseases or pathological conditions

clinical biochemistry

studies microbes

bacterial biochemistry

studies plants

plant biochemistry

studies animals


animal biochemistry

studies industrial products involved with microorganisms

industrial biochemistry

smallest unit that is capable of performing life functions

cell

all living things are made up what?

cells

cells come from pre existing cells through

cell division

types of cells

prokaryotic


eukaryotic

this cell do not have structures surrounded by membranes

prokaryotic

this cell only has fe internal structure

prokaryotic

one-celled organism

prokaryotic

this cell has no nucleus

prokaryotic

this cell contains organelles surrounded by membranes

eukaryotic

most living organisms are composed of this cell

eukaryotic

a subcellular structure that has one or more specific jobs to perform in the cell

organelles

surrounded by cell membrane and cell wall

organelles

outer membrane of the cell; controls movement in and out of the cell; double layer

cell membrane

found in plant cells and bacteria; supports and protects cells

cell wall

directs all cell activities; separated from cytoplasm by nuclear membrane; contains dna

nucleus

surrounds nucleus; 2 layers; allows material to enter and leave the nucleus

nuclear membrane

located in the nuclear; made of dna; contain instructions for traits and characteristics

chromosomes

located inside the nucleus; contains rna to build proteins

nucleolus

a gel-like mixture; surrounded by cell membrane; contains hereditary material such as genetic information

cytoplasm

moves materials around in the cell; has 2 types- smooth and rough

endoplasmic reticulum

a type of ER that lacks ribosomes

smooth

a type of ER that has ribosomes embedded on the surface

rough

there are thousands pf this in the cell; make proteins; floating throughout the cell

ribosomes

produces energy through chemical reactions; controls water level and other materials; recycles and decomposes proteins, fats, and carbohydrates

Mitochondria

digestive plant for proteins, fats, and carbohydrates; transports undigested materials to cell membrane

lysosomes

membrane bound sacs for storage, digestion, and waste removal; contains water solution; help plants maintain shape

vacuoles

found in plant cells; green chlorophyll; site for photosynthesis

chloroplast

this is produced by living organisms

biomolecules

made up of compound carbon

biomolecules

building blocks of life

biomolecules

what are the 4 biomolecules

carbohydrates


lipids


proteins


nucleic acids

monomer of carbohydrates

simple sugar

monomers of lipids

glycerol and fatty acids

monomer of proteins

amino acids

monomer of nucleic acid

nucleotide

atoms of water

H2O

the atoms of water are held together by a

polar covalent bond

shape of the water molecule

bent (mickey mouse)

7 properties of water

polarity


capillary action


surface tension


heat capacity


heat of vaporization


density


universal solvent

positive and negative charged ions

polarity

the ability of water to flow upward against the force of gravity due to cohesion and adhesion

capillary action

cohesion

sticking together of two like molecules

adhesion

sticking together of two unlike molecules

a measure of the force necessary to stretch or break the surface of a liquid

surface tension

amount of heat that must be absorbed or lost before it actually changes temperature

specific heat

the cooling of a surface occurs when the liquid evaporates

heat of vaporization

measure of how compact the atoms or molecules are within a substance or how much mass there is in a given space

density

water is solvent

universal solvent

dissolves particles

solvent

gets dissolved

solute

are macromolecules composed of amino acids linked together through peptide bonds

proteins

one of the 20 a-amino acids normally found in proteins

standard amino acids

an organic compound that contains both amino (-NH2) group and a carboxyl (-COOH) group

amino acid

an amino acid in which the amino group and the carboxyl group are attached to the alpha carbon atom

alpha amino acid

structure of amino acid

the same for all amino acids

back bone

2 groups present in amino acids in the same molecules

carboxyl and amino group

amino acids found in proteins

alpha amino acids

always found on the carbon adjacent to the carboxyl group

amino group

also called side chains which make each AA unique and distinctive

R groups

grouped as non polar hydrophobic polar neutral basic and acidic

AAs

glycine alanine valine leucine isoleucine

aliphatic

proline

cyclic

phenylalanine tyrosine tryptophan

aromatic

serine threonine tyrosine

hydroxyl containing

cysteine methionine

sulfur-containing

histidine lysine arginine

basic

aspartic acid glutamic acid asparagine glutamine

acidic and their amides

classification of amino acids according to the side-chain polarity

nonpolar amino acid


polar neutral amino acid

contains one amino group and one carboxyl group and non-polar side chain hydrophobic 9 nonpolar amino acids

nonpolar amino acid

contains one amino group one carboxyl group and a side chain that is polar but neutral six amino acids

polar neutral amino acid

R groups are nonpolar hydrophobic-aliphatic or aromatic groups



r groups are and charged



aasar in soluble in h2o

nonpolar and hydrophobic aas

R groups are polar: -OH, -SH, -NH2



R groups are highly reactive



AAs are soluble in h2o that is hydrophilic

polar and uncharged aas

this one amino group and to carboxyl groups the second carboxyl group being part of the side chain



(2AA) the side-chain bears a negative charge

polar acidic amino acid

contains two amino groups and one carboxyl group the second amino group being part of the side chain (3AA) the side-chain bears a positive charge

polar basic amino acid

Basic AAs

Acidic AAs

examples of acidic amino acids

examples of basic amino acids I

examples of basic amino acids II

no of essential amino acids

10

no of nonessential amino acids

10

essential amino acids

nonessential amino acids

complete protein

incomplete protein

non-superimposed molecules



mirror image



four different group bounded to the alpha carbon

chirality

except for glycine all amino acids have

chiral carbon atom, have optical isomers

the amino acids found in proteins are all

levorotatory or L forms

have a tendency to lose protons H+ producing a negatively charged species

carboxyl groups

have a tendency to accept protons H+ juicing positively charged species

amino groups


capability of behaving as both an acid and a base since they have both a proton donor group and a proton acceptor group

amphoteric

dipolar ion form

zwitterion

a molecule that has a positive charge on one atom and a negative charge on another atom but which has no net charge

zwitterion

in this solution, the zwitterion accepts a proton to form a positively charged ion

acidic solution

in this solution the NH3 of the zwitterion loses a proton and a negatively charged species is formed

basic solution

three different amino acid in a solution

zwitterion negative ion and a positive ion

is the ph at which an amino acid solution has no net charge because an equal number of positive and negative charges are present

isoelectric point

is the process of separating charged electrode associated with an electric field

electrophoresis

unbranched chain of amino acid

peptide

how is a peptide classified

by the number of amino acids present in the chain

a type of peptide that contains two amino acids

dipeptide

a type of peptide that contains three amino acid

tripeptide

a type of peptide that has 10 to 20 amino acids

oligopeptide

a type of peptide that has more than 20 amino acids and is a long on branched chain of amino acids each joined to the next by a peptide bond

polypeptide

it is a covalent bond formed between the carboxyl group of one amino acid and the amino group of its next amino acid with the elimination of one h2o molecule

peptide bond

is formed and lost when two amino acids combine

amide and water molecule

working molecule of the cell

protein

function of protein

building of new cells


maintenance of existing cells


replacement of old cells

function of protein



regulation of

metabolic processes

function of protein



catalysis of

biochemical reactions

function of protein



transportation of

oxygen (hemoglobin) in blood


and in the muscle (myoglobin)

classification of proteins according to shape

globular - ball


fibrous - rod

biochemical catalyst called enzymes

catalytic protein

classification of proteins based on function

antibodies, central to functioning of the body's immune system

defense protein

classification of proteins based on function

hemoglobin

transport proteins

classification of proteins based on function

transmit signals


insulin

messenger proteins

classification of proteins based on function

collagen

structural proteins

classification of proteins based on function

bind small molecules for future use


myoglobin

storage proteins

classification of proteins based on function

important in the early stages of lie from embryo to infant



casein in milk

nutrient proteins

composed of only amino acid unit and on hydrolysis yield only amino acids

simple protein

classification of proteins according to composition

contain another type of molecule or compound attached to the amino acid unit and on hydrolysis yield amino acids and that other molecule

conjugated proteins

classification of proteins according to composition

secondary

level of structure of protein

refers to the complex conformations that result from the extensive bending and folding of protein chains that characterizes globular proteins

tertiary

level of structure of protein

occurs when 2 or more protein units combine to form a more complex unit

quaternary

level of structure of protein

denatured proteins tend to

protein packaging plant; move materials out of the cell

golgi bodies