Module 2 - Anatomy Flashcards

1
Q

ionic bond

A

attraction between oppositely charged ions: cation (+) and anion (-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

covalent

A

the sharing of a pair of valence electrons by 2 atoms
1) non-polar: electrons equally shared
2) polar: electrons shared unequally

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

hydrogen bonds

A

attraction between partially positively charged hydrogen atoms and partially negatively charged electronegative atoms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

macromolecules

A

1) carbohydrates
2) proteins
3) lipids
4) nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Macromolecules

A
  • they are all organic
  • mostly CHO atoms
  • High carbon content
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

why carbon?

A
  • common
  • 4 valence electrons
  • bonds to other carbons to form complex backbones
  • forms covalent bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

reactions to make and break polymers

A

1) dehydration synthesis/condensation
2) hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

dehydration synthesis/condensation

A

1+1=2
product: water + polymer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

hydrolysis

A

2=1+1
reactant: water + polymer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

carbohydrates: function

A
  • carbohydrates are a quickly mobilized source of energy
  • all digested carbohydrates converted to glucose
  • oxidized to make ATP
  • carbohydrates are often conjugated with:
    1) lipids -> glycolipids
    2) proteins -> glycoproteins
  • proteoglycans are more carbohydrate than protein
    1) gels that hold cells and tissues together; fill the umbilical cord and eye
    2) joint lubrication: responsible for the rubbery texture of cartilage
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Phospholipids

A

Amphipathic
- hydrophilic heads
- hydrophobic tail

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

eicosanoids

A
  • function primarily as chemical signals between cells (cellular communication)
  • prostaglandins: inflammation, pain, blood clotting
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

steroids

A
  • lipids in which the carbon skeleton contains 4 fused rings
  • cholesterol = 4 ring parent steroid
    1) importance structural component of cellular membranes
    2) starting material for making steroid hormones (communication): cortisol, testosterone, estrogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

amino acid

A

central carbon bonding with
1) an amino group
2) a carboxyl group
3) a hydrogen atom
4) a functional group R
classified as:
- hydrophilic
- hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

dipeptide

A

proteins are made from amino acids linked by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

polypeptide

A

peptides are names for the number of amino acids they contain:
- dipeptides (2 amino acids)
- tripeptides (3 amino acids)
- oligopeptides (btwn 3 and 15 amino acids)
- polypeptides btwn 15 and 50 amino acids)
- proteins (more than 50 amino acids)

17
Q

primary structure

A
  • the unique linear sequence of amino acid that determines all other levels of structure
  • results from the formation of peptide bonds between amino acids
18
Q

Secondary structure

A
  • the two dimensional shape: the coiling (alpha helix) or folding (beta-pleated sheet) of the polypeptide
  • results from the formation of hydrogen bonds between atoms of the polypeptide backbone
19
Q

Tertiary structure

A
  • the three-dimensional shape
  • results from interactions between the R groups of the various amino acids (disulfide bridges)
20
Q

Quaternary structure

A
  • the association of 2 or more polypeptide chains
  • results from ionic bonds and hydrophobic interactions
21
Q

enzymes

A
  • proteins
  • biological catalysts
  • lower activation energy of reactions
  • increase the rate of a reaction without being consumed by the reaction (neither reactants nor products)
  • highly specific
22
Q

enzyme proteins

A

serve as metabolic catalysts and regulate chemicals

23
Q

structural proteins

A

provide associations between body parts

24
Q

contractile proteins

A

are found within muscles

25
defensive proteins
include antibodies of the immune system
26
signal proteins
best exemplified by hormones and other chemical messengers
27
receptor proteins
transmit signals into cells
28
transport proteins
carry oxygen
29
storage proteins
serve as a source of amino acids for developing embryos
30
nucleotides
1) five-carbon sugar 2) phosphate group 3) nitrogenous base
31
DNA
Adenine (A) Thymine (T) Cytosine (C) Guanine (G)
32
RNA
Adenine (A) Cytosine (C) Guanine (G) Uracil (U)
33
Adenosine Triphosphate
Consists of - the nitrogenous base adenine - the five-carbon sugar ribose - three phosphate groups Holds energy in covalent bonds - second and third phosphate groups have high energy bonds - most energy transfers to and from ATP involve adding or removing the third phosphate group The body's most important energy transfer molecule - stores energy gained from exergonic reactions - releases it within seconds for physiological work
34
ATP drives cellular work
- by coupling exergonic and endergonic reactions - in the ATP cycle, energy released in an exergonic reaction, such as the breakdown of glucose, is used in an endergonic reaction to generate ATP
35
ATP powers cellular work
1) chemical 2) mechanical 3) transport