Human Physiology Ch 2

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1

types of chemical bonds

covalent

ionic

hydrogen

2

covalent bonds

molecules share electrons

strongest bond

3

nonpolar covalent bonds

molecules share electrons equally

4

polar covalent bonds

molecules share electrons unequally

5

ionic bonds

one atom takes an electron, one atom gives electron

6

ions

atoms with unequal numbers of protons to electrons

7

cation

positively charged ion

8

anion

negatively charged ion

9

ionic bond

strong electrostatic attraction between oppositely charged ions

10

can ionic bonds dissassociate in water

yes, because they are weaker than covalent bonds

11

hydrogen bond

weak attraction between polar molecules

12

polar molecules

may dissolve in water and are called hydrophilic

13

nonpolar molecules

cannot dissolve in water and are called hydrophobic

14

hydrophilic

water soluble

polar molecules and ions

15

hydrophobic

water insoluble

nonpolar molecules

16

acids

release hydrogen into solutions

17

bases

bind hydrogen in water

18

pH

acidity scale

lower number = higher acidity

7 is neutral

higher number = more basic

19

4 types of macromolecules

proteins

lipids

carbohydrates

nucleic acids

20

carbohydrates

sugars and starches

21

monosaccharides

one carbon ring

22

disacharides

two monosaccharides bound together via covalent bond

23

polysaccharides

many monosaccharides bound together

ie starch and glycogen

24

lipids

generally hydrophobic

25

3 major classes of lipids

triglycerides

phosopholipids

steroids

26

triglyceride structure

2 fatty acids attached to a glycerol backbone

27

2 types of fatty acids

saturated and unsaturated

28

phosopholipid

amipathic=possess polar and nonpolar ends

29

prostaglandins

Serve as communicaton molecules between cells in the same organ

30

amino acids

building blocks of acids

20 total

11 essential, 9 nonessential

31

amino acid structure

amino group

carboxyl group

function side chain

32

peptide bond

Covalent bond linking the carboxyl group of one amino acid to the amino group of the next

33

polypeptide

molecule made of many peptide bonds

34

protein structure

primary structure-sequence amino acids in a polypeptide chains

35

protein secondary structure

formation of helix or sheet shape due to amino acid attractions

36

protein tertiary structure

twisting and folding of peptide chain

3D shape

37

quarternary protein structure

bonding of peptide chains

38

protein functions

antibodies

structure

enzymes

receptors

carriers

39

DNA structure

sugar=deoxyribose

double helix-Two strands linked together by hydrogen bonds between nitrogenous bases

40

complimentary base pairs in DNA

adenine binds to thymine

guanine binds to cytosine

41

RNA

ribonucleic acid

usually single stranded

different sugar than DNA (ribose)

different nitrogen base (uracil instead of thymine)

42

three types of RNA

mRNA-messenger

tRNA-transfer

rRNA-ribosomal