Organic Compounds Flashcards

1
Q

iosmers

A

org. compounds w/ same mol. formula, but different structures which cause them to have different prop.

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

types of isomers

A

structural isomers, cis-trans isomers. enantiomers

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

structural isomers

A

differ in arrangement of atoms

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

cis-trans isomers

A

differ in spatial arrangement around double bonds (not flexible like single bonds)

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

enantiomers

A

molecules that are mirror images of each other, (left handed L- and right handed D-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

L- vs D- fact

A

mirror images may not be equally effective, L- dopa is useful for treatment of Parkinson’s but D- dopa is not biologically active

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Q: amino acids in cells are left or right handed?

A

all amino acids are left handed.

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

org. compounds

A

all living organisms have them, contain carbon

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

four classes of organic compounds

A

carbohydrates, lipids, proteins and nucleic acids

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

Carbohydrates

A

body uses as fuel and building materials

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

carbs constituent elements

A

C, H, O

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

ratio of H to O in all carbs

A

2:1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

carbs == QUICK energy

A

1 gram of any carb == 4 calories when burned with a calorimeter

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

3 classes of carbohydrates

A

monosaccharides, disaccharides, and polysaccharides

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

monosaccharides

A

Chemical formula: C6H12O6, ex: glucose, galactose, and fructose, all isomers

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

conventional numbering of C in rings

A

numbering begins to the right of O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

disaccharide

A

chemical formula: C12H22O11, two monosacc. together with a release of 1 H20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

dehydration synthesis or condensation

A

process of joining two molecules by releasing a H20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

glucose + glucose

A

maltose + water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

glucose + galactose

A

lactose + water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

glucose + fructose

A

sucrose + water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

hydrolysis

A

break down of a compound by adding water, reverse of condensation synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Q: sucrose + water –> glucose + fructose is an example of what?

A

hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

monosaccharide + monosaccharide –>

A

disaccharide + h20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
polysaccharides
macromolecules, polymers of carbohydrates, formed by many monosaccharides joined together by dehydration
26
Q: What process enables monosaccharides to join together to form polysaccharides?
dehydration
27
Q: What are the structural polysaccs found in plants and animals?
cellulose (plant cell walls) and chitin (exoskeleton in arthropods and cell walls in fungi)
28
Q: What are the structural polysaccs found in plants and animals?
starch (forms are amylose and amylopectin) and glycogen (animal starch stored in liver and skeletal muscle)
29
4 things that are included under lipids
fats, oils, waxes, and steroids
30
structural components of most lipids
1 glycerol and 3 fatty acids
31
fatty acid
hydrocarbon chain with a carboxyl group at one end
32
2 varieties fatty acids
saturated and unsaturated
33
saturated fats prop. and example
generally come from animals, solid at room temp. and when ingested in large quantities are linked to heart disease, ex: butter
34
bonds in sat. fats
single bond
35
unsaturated fats prop. and example
extracted from plants, liquid at room temp, healthy dietary fats
36
bonds in unsaturated fats
atleast one double bond formed by removal of H atoms, usually have fewer H atoms than sat fats
37
exception to unsat. fats having less H atoms than sat fats
coconut and palm oil that are saturated
38
steroids
don't have same general structure as other lipids, instead have 4 fused rings
39
steroid examples
testosterone and estradiol
40
functions of lipids
energy storage, structural, endocrine
41
energy storage
1 gram of lipid --> 9 calories, 2x as much as proteins or carbs
42
structural
phospholipids (where phosphate group replaces one fatty acid) are major component of cell membrane, cholesterol is an important component of plasma membrane of animal cells
43
endocrine
some steroids are hormones
44
phospholipids
only 2 fatty acids attached to glycerol backbone, forming two hydrophobic tails
45
phospholipid head
has the phosphate and glycerol, phosphate is charged, therefore hydrophilic, when arranged into membrane, stays on the outside
46
proteins
complex unbranched molecules, polymers or polypeptides consisted of units called amino acids, which are joined by peptide bonds
47
protein functions
growth and repair, signaling form one cell to another, regulation: hormones such as insulin lower blood sugar, enzymatic activity: catalyzing chemical reactions, movement: actin and myosin are protein fibers responsible for muscle contractions
48
dietary sources of protein
fish, poultry, meat, plants like beans and peanuts
49
1 gram of pro. ==
4 cal
50
elements of proteins
CHNOPS
51
amino acids consist of
carboxyl group amine group and R variable attached to a central asymmetric carbon atom
52
r group
differs with each amino acid, interactions among r groups ultimately determine structure and function of protein
53
fun fact: with only 20 amino acids
cells can build thousands of proteins
54
two amino acids with dehydration synthesis
form dipeptide, or molecule with two amino acids with one peptide bond
55
conformation
shape that determines job performed
56
four levels of protein structure that are responsible for protein's conformation
primary, secondary, tertiary, and quaternary
57
primary structure of a protein
refers to the unique linear sequence of amino acids, a slight change in the amino acid sequence can have major consequences
58
Q: sickle cell anemia is caused by the switcharoo of what
substitutes valine(GTG) for glutamic(GAG) acid in a molecule of hemoglobin
59
Q: During the 1940s and 50s who was the first man to sequence a protein
Fred Sanger
60
What protein did Sanger first sequence and what reward did he receive
He sequenced insulin, and received the nobel prize
61
secondary structure
results from hydrogen bonding within the polypeptide molecule, refers to how the polypeptide coils or folds
62
two distinct secondary structures
alpha helix and beta pleated sheet
63
fibrous proteins
proteins that exhibit either alpha helix or beta-pleated sheets or both
64
ex. of fibrous proteins
wool, claws, beaks, reptile scales, collagen and ligaments
65
Q: keratin (human hair) is made up of mostly this protein type
alpha helizs
66
Q: Silk and spider webs consist of this protein type
beta-pleated sheets
67
tertiary structure
intricate 3d shape or conformation of a protein that is superimposed on its secondary structure
68
tert. struc. determines
protein's specificity
69
factors that contribute to tert. struct.
H bonding btw R groups of amino acids, ionic bonding btw r groups, hydrophobic interactions, Van der Waals interactions, disulfide bonds btw cysteine amino acids
70
quaternary structure
proteins that consist of more than one polypeptide chan
71
hemoglobin fact about quat. struct
exhibits quat struct. bc it consists of 4 polypeptide chains each forming a heme group
72
specificity def.
Chemical specificity is the ability of a protein's binding site to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand.
73
factors affecting protein shape, folding
pH, salt concentration, temp
74
denaturation
these external factors can affect the weak intramolecular forces causes the protein to lose its shape and thus function this is called denaturation
75
basic concept of modern bio
protein conformation affects function
76
chaperone proteins or chaperonins
assist in folding other proteins
77
prions
accumulations of misfolded proteins in brain cells
78
diseases caused by prions
Alzheimer's, Parkinson's, and mad cow disease
79
3 complementary techniques used to reveal the 3d shape of proteins
X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and bioinformatics
80
bioinformatics
uses comps and math modeling to integrate the huge volume of data to predict the 3d model of the structure
81
2 nucleic acids
RNA and DNA
82
nucleic acid fuction
encode all hereditary information
83
Q: info encoded in the sequence of nucleotides in DNA specifies
the amino acid sequences of all proteins
84
nucleotide consists of
phosphate, 5C sugar (deoxyribose or ribose), and a nitrogen base, (Adenine, Thymine, Cytosine, Guanine, or Uracil)
85
components of org. mol. that are most involved in chemical reactions
functional groups
86
how funct. groups are attached
to the C skeleton, replacing one or more H atoms
87
Amino group
compound name: amino, H-N-H
88
Carboxyl group
compound name: carboxyl, O--C-OH
89
Hydroxyl group
compound name: alcohol, OH
90
Phosphate group
compound name: phosphate, O--P-O-O-O