Bio Exam 1 review

what is the process of learning?

stimulus - sensory memory - STM - LTM

the storage of sensory memory

temporary storage from 5 sense

the storage of STM

brief storage of info being used currently

the storage of LTM

Permanent storage for info not being used at that moment

the capacity of sensory memory

high

the capacity of STM

7 +/- 2 memories

the capacity of LTM

unlimited

duration of sensory memory

less than 1 second for vision and a few seconds for hearing

duration of STM

less than 20 seconds

duration of LTM

permanent as long as LTP is present

Type of sensory memory

declarative knowledge

type of STM

attention while in lecture

type of LTM

repetition of info, practice

neuronal development

brain develops and grows after birth (embryonic development)

neural plasticity

brain is changed after birth - synapses

activity dependent

lots of activity - more connections

themes of biology

emergence and reductionism

biological organizer levels

organelles - cells - tissue- organs/organ systems - organisms/populations/communities - ecosystem - biosphere

scientific method

observation - background - hypothesis/predictions - experiment - evaluate

what happens if once repeated and verified was unsuccessful?

go back to predictions

what happens if incorrect predictions?

revise predictions and hypothesis

what happens if repeat and verify is successful?

ask a new question

charge of proton

\+

charge of electron

\-

charge of neutrons

neutral

location of proton

nucleus

location of electron

orbitals

location of neutrons

nucleus

role of electrons

reactions

role of protons

identity + mass

role of neutrons

mass

non polar covalent bonds with?

atoms

polar covalent bonds with?

between atoms

ionic bonds with?

between atoms

Van Der Waals (HB) binds with

between molecules

non polar covalent bonds sharing?

equal share with e-

polar covalent bonds sharing?

unequal share with e- , partial +/- charge

ionic bond sharing?

stealing or transferring of e-

Van Der Waals (HB) sharing?

interaction between molecules

non polar covalent bond strength

strongest

polar covalent bond strength

strong

ionic bond strength

weak

Van Der Waals (HB) strength

weakest

electronegativity of non polar covalent bonds

same

electronegativity of polar covalent bonds

electronegativity of ionic bonds

>2

electronegativity of Van Der Waals (HB)

N/A

emergent properties of water

hydrogen bonding, cohesive behavior, moderate tempature, expansion upon freezing

hydrogen bonding

• bond pairing water molecules together

• leads to 4 other properties

cohesive behavior

• cohesion

• adhesion

• surface tension

cohesion

water sticking together - dome

adhesion

water sticking to other polar things - rain on window

surface tension

hard to break tension - spider

moderate tempeture

high specific heat

expansion upon freezing

ice floats - air pockets from hydrogen bonds

versatility as solvent

hydrophilic and hydrophobic

hydroxyl group

\-OH

Hydroxyl characteristics

polar, hydrophilic, neutral

carbonyl group

\-CHO or C=O

carbonyl characteristics

polar, hydrophilic, neutral

carboxyl group

\-COOH

carboxyl characteristics

polar, hydrophilic, acid

Amino Group

\-NH2

amines characteristic

polar, hydrophilic, base

sulfhydryl group

\-SH

Thiol characteristics

polar, hydrophilic, slightly acid

phosphate group

\-PO4H2

phosphate characteristic

polar, hydrophilic, acid

methyl group

\-CH3

methyl characteristics

non-polar, hydrophobic, neutral

biological macromolecules

carbohydrates, lipids, proteins, nucleic acids

what are carbs made of?

hydrocarbons

what are lipids made of?

fatty acids, glycerol

what are proteins made of?

amino acids

what are nucleic acids made of?

nucleotides

function of carbohydrates

storage and structure

function of lipids

energy storage

function of proteins

structure, signaling, transport, defense

function of nucleic acids

genes and heredity

monomers of carbohydrates

monosaccharides

monomers of proteins

amino acids

monomers of nucleic acids

nucleotides

polymer of carbohydrates

disaccharide, polysaccharides

polymer of proteins

polypeptide

polymer of nucleic acids

DNA, RNA, ATP

bonds of carbohydrates

glycosidic linkage

bonds of lipids

ester linkages

bonds for proteins

peptide bonds

bonds for nucleic acids

phosphodiester bonds

protein stucture

primary, secondary, tertiary, quaternary

primary protein structure

linear chain of amino acids

secondary protein structure

folding of polypeptide, α helix or β folded sheets

tertiary protein strcture

3D shape

quaternary protein structure

joining of additional polypeptide chains

bonds in primary protein structure

peptide bonds

bonds in secondary protein structure

hydrogen bonds

bonds in tertiary protein structure

all types

bonds in quaternary protein structure

all types

denaturation occurs when?

3rd and 4th stage of protein structure

dehydration synthesis

removes H2O to join together - makes polymers