ch 1- molecules and fundamentals of biology Flashcards

(91 cards)

1
Q

the smallest unit of matter that stil retains the chemical properties of the element

A

atom

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2
Q

pure substances with specific chemical and physcal propertiesthat cannot be broken down into a simpler substance

A

element

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3
Q

anything that takes up space and has mass

A

matter

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4
Q

forces that affect physical properties of a substance

A

intermolecular

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5
Q

uses of carbs

A

structural supportwh

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6
Q

what elements are in carbs

A

carbon
hydrogen
ocygen

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7
Q

monosaccharide rings

A

a and B sugar

a- OH on either side of -O- are on SAME SIDE
B- OH on either side of -O- are on OPPOSITE SIDES

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8
Q

ribose

A

5 carbon monosacharide

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9
Q

fructose

A

6 carbons

monosaccharide
glucose structural isomer

both hexose

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10
Q

what are disaccharides connected by

A

a glycosidic bond/ covalent bond

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11
Q

sucrose

A

disaccharide

glucose and fructose

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12
Q

lactose

A

disaccharide

galactose and glucose

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13
Q

maltose

A

disaccharide

glucose and glucose

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14
Q

function of starch

A

energy storage for plants

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15
Q

form of starch

A

a bonded polysaccharide

linear (amylose) and branched form (amylopectin)

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16
Q

glycogen structure and function

A

energy storage in animals

a bonded polysaccharide

MUCH MORE BRANCHING THAN STARCH

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17
Q

what differs branched polysaccharides from linear ones

A

branched has a-1,6 and 1,4 glycosydic bonds while linear only has a-1,4 glycosidic bonds

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18
Q

how is glucose stored long term

A

as glycogen in the muscles and liver

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19
Q

chitin

A

polysacharide that is parallel structure

B1,4 glycosydic bond

N containing groups replace one of the cellulose OH groups

polymer of N acetyl glucosamine

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20
Q

cellulose

A

a-1,4

srong H bonds

glucose monomers

parallel structure

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21
Q

what atoms are in proteins

A

carbon
nitrogen
hydrogen
oxygen

CHON

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22
Q

proteome

A

all proteins ecrpressed by ONE TYPE OF CELL under CERTAIN CONDITIONS

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23
Q

what are the monomers of proteins

A

amino acids

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24
Q

what joins two amino acids

A

peptide bonds

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25
conjugated proteins
amino acids and non protein components metalloproteins glycoproteins
26
metalloproteisn
conjugated protein ex hemoglobin contain metal ion cofactor
27
glycoprotein
conjugated protein contains carbohydrate group ex, mucin
28
primary structure of proteins
amino acids and peptide bonds
29
secondary structure proteins
IM forces bw protein backbone NOT R GROUP Hydrogen bonding a helices and B sheets
30
tertiary structure proteins
interactions between R groups (H bond, ionic, disulfide) 3D hydrophobic interactions disulfide bonds (covalent interactions bw cysteines)
31
quaternary structure protein
multiple polypeptide chains
32
what remains after protein denaturation
loss of structure and higher order only primary structure unaffected SOME CAN REVERSE
33
what causes denturation
high or low temps salt concentrations pH changes
34
transition state
unstable conformatino
35
catalysts
reduce the energy of transition state and actiation energy of reactions DONT SHIFT CHEMICAL REACTION OR AFFECT SPONTENAITY
36
enzymes
biological catalysts work by induced fit conformational changes bringing reactants closer acidic or basic groups electrostatic attractions bc enyme and substrate
37
what substances are enzymes
most are proteins, ribozymes are made from RNA not proteins but theyre enzymes
38
what does the specificity constant measure
how efficeint an enzyme is to binding to a substrate
39
induced fit theory vs lock and key thoery
induced fit is right lock and key is outdated
40
cofactor
non protein molecule that helps enzymes inorganic cofactors- metal ions organic cofactors- vitamins
41
coenzyme
organic cofactor ex, vitamins
42
holo vs apoenzyme
holoenzyme- bound to cofactor apoenzyme- enzymes NOT bound to cofactors
43
prosthetic group
cofactors tightly or covalently bound to enzymes
44
phosphatase
cleaves phosphate groups off a substrate molecule
45
phosphorylase
directly adds phosphate group by brakig bonds within substrate molecule
46
kinase
indirectly adds a phosphate groups transfers phosphate group from ATP molecule DO NOT BREAK BONDS to add phosphate
47
what does an enzyme kinetics plot visualize x and y axis
how inhibitors affect enzymes x- substrate conc y- reaction rate/ velocity
48
Km
substrate conc that recation velocity is 50% of Vmax
49
competitive inhibition
Km inc V max stays same
50
non competitive inhibition
V max dec Km stays the same
51
what atoms are in lipids
carbon hydrogen oxygen
52
glycerol backbone
threee carbons and three hydroxyl groups
53
what connects the glycerol backbone and three fatty acid
ester linkages
54
phospholipid structure
glycerol backbone one phosphate group (polar) ` two fatty acid tails
55
amphipathic molecules
phospholipids cholesterol glycolipids
56
what is cholesterol a precursor for
steroid hormones- four rings made from cholesterol vitamin D bileq
57
where is cholesterol found
lipid membranes
58
temp and membrane fliuidity
high temp inc fluidity low temp dec it
59
cholesterol and fluidity of membranes
keeps membranes tog at high temp and separated at low temp
60
low density lipoprotieins protein content
low protein conent
61
LDL function
cholesterol from liver to peripheral tissue
62
HDL function
cholesterol from peripheral tissue to liver
63
waxes
lipids with long FA chains connected to monohydroxyl alcohols through ester linkages
64
cartenoids
lipid derivative long chain conjugated double bonds six membered rings at each end pigments
65
sphignolipids
have backbone with aliphatic amino alcohols structural support signal transduction cell recognition
66
aliphatic meaning
non aromatic
67
glycolipids
lipids with a carb group replacing phosphate in membrane of cells amphipathic
68
atoms in nucleic cids
CHONP carbon hydrogen oxygen nitrogen phosphorus
69
nucleoside
5 carbon sugar and nitrogenous base
70
nucleotide
5 carbon sugar nitrogenous base phosphate group
71
difference between DNA and RNA
DNA- H at 2' carbon and OH at 3' RNA- OH group at 2' and 3' group
72
purines
two rings adenine guanine
73
pyrimidines
one ring thymine uracil cytosine
74
what connects two nucleotides tog
phosphodiester bonds phosphate of 5' carbon and OH of 3' carbon
75
A and T H bonds
2
76
G and C H bonds
3
77
miRNA
small RNA that silences gene expressionb by base pairing to complementary sequesnces on mRNA
78
rRNA where is it formed
nucleolus helps ribosomes translate mrNA
79
dsRNA
some viruses carry genetic code in this must have equal amounts of A/U and G/C
80
how old is the universe
approx 13.8 billion years old
81
when did first cells appear on earth
3.5 billion years ago
82
primordial earth
- first atmosphere- inorganic compounds- reducing enviroment- little 02 - earth cooled- gasses condensed- primordial sea formed - simple compounds -> more complex organic compounds - monomers-> polymers -probionts emerged (precursors to cells) - heterotroph obligate anaerobe prokaryotes emerged - autotroph prokaryotes emerged (cyanobacteria)- o2 accumulation - primitive euk emerged - endosymbiotic theory -more complex euk emerged
83
modern cell theory
all lifeforms have one or more cells cell is basic structural, functional, and organizational unit of life all cells from from other cells genetic info is stored and passed odwn through DNA an organisms activty is dependant on total actiivty of its cells metabolism and biochemistry occcur within cells all cells have same chemical composition within organisms of similar species
84
central dogma of genetics
info is passed from DNA to RNA to proteins can interconvert bw DNA +DNA, RNA+ RNA, from RNA to DNA and proteins to proteins (prions) reverse transcriptase is an exception and so are prions
85
RNA world hypotheiss
early life forms relied on self replicating RNA to store genetic info and catalyze chemical reactions DNA is more stable so replaced in genetic storing and Proteins replaced the catalytic function
86
what does peri mean
around
87
bast meaning
formative cell
88
plasia meaning
development/ formation
89
scopy meaning
examination/ inspection
90
stasis meaning
stopping
91
trophy meaning
growth