Organic Compounds Flashcards
iosmers
org. compounds w/ same mol. formula, but different structures which cause them to have different prop.
types of isomers
structural isomers, cis-trans isomers. enantiomers
structural isomers
differ in arrangement of atoms
cis-trans isomers
differ in spatial arrangement around double bonds (not flexible like single bonds)
enantiomers
molecules that are mirror images of each other, (left handed L- and right handed D-)
L- vs D- fact
mirror images may not be equally effective, L- dopa is useful for treatment of Parkinson’s but D- dopa is not biologically active
Q: amino acids in cells are left or right handed?
all amino acids are left handed.
org. compounds
all living organisms have them, contain carbon
four classes of organic compounds
carbohydrates, lipids, proteins and nucleic acids
Carbohydrates
body uses as fuel and building materials
carbs constituent elements
C, H, O
ratio of H to O in all carbs
2:1
carbs == QUICK energy
1 gram of any carb == 4 calories when burned with a calorimeter
3 classes of carbohydrates
monosaccharides, disaccharides, and polysaccharides
monosaccharides
Chemical formula: C6H12O6, ex: glucose, galactose, and fructose, all isomers
conventional numbering of C in rings
numbering begins to the right of O
disaccharide
chemical formula: C12H22O11, two monosacc. together with a release of 1 H20
dehydration synthesis or condensation
process of joining two molecules by releasing a H20
glucose + glucose
maltose + water
glucose + galactose
lactose + water
glucose + fructose
sucrose + water
hydrolysis
break down of a compound by adding water, reverse of condensation synthesis
Q: sucrose + water –> glucose + fructose is an example of what?
hydrolysis
monosaccharide + monosaccharide –>
disaccharide + h20
polysaccharides
macromolecules, polymers of carbohydrates, formed by many monosaccharides joined together by dehydration
Q: What process enables monosaccharides to join together to form polysaccharides?
dehydration
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)
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)
4 things that are included under lipids
fats, oils, waxes, and steroids
structural components of most lipids
1 glycerol and 3 fatty acids
fatty acid
hydrocarbon chain with a carboxyl group at one end
2 varieties fatty acids
saturated and unsaturated
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
bonds in sat. fats
single bond
unsaturated fats prop. and example
extracted from plants, liquid at room temp, healthy dietary fats
bonds in unsaturated fats
atleast one double bond formed by removal of H atoms, usually have fewer H atoms than sat fats
exception to unsat. fats having less H atoms than sat fats
coconut and palm oil that are saturated
steroids
don’t have same general structure as other lipids, instead have 4 fused rings
steroid examples
testosterone and estradiol
functions of lipids
energy storage, structural, endocrine
energy storage
1 gram of lipid –> 9 calories, 2x as much as proteins or carbs
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
endocrine
some steroids are hormones
phospholipids
only 2 fatty acids attached to glycerol backbone, forming two hydrophobic tails
phospholipid head
has the phosphate and glycerol, phosphate is charged, therefore hydrophilic, when arranged into membrane, stays on the outside
proteins
complex unbranched molecules, polymers or polypeptides consisted of units called amino acids, which are joined by peptide bonds
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
dietary sources of protein
fish, poultry, meat, plants like beans and peanuts
1 gram of pro. ==
4 cal
elements of proteins
CHNOPS
amino acids consist of
carboxyl group amine group and R variable attached to a central asymmetric carbon atom
r group
differs with each amino acid, interactions among r groups ultimately determine structure and function of protein
fun fact: with only 20 amino acids
cells can build thousands of proteins
two amino acids with dehydration synthesis
form dipeptide, or molecule with two amino acids with one peptide bond
conformation
shape that determines job performed
four levels of protein structure that are responsible for protein’s conformation
primary, secondary, tertiary, and quaternary
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
Q: sickle cell anemia is caused by the switcharoo of what
substitutes valine(GTG) for glutamic(GAG) acid in a molecule of hemoglobin
Q: During the 1940s and 50s who was the first man to sequence a protein
Fred Sanger
What protein did Sanger first sequence and what reward did he receive
He sequenced insulin, and received the nobel prize
secondary structure
results from hydrogen bonding within the polypeptide molecule, refers to how the polypeptide coils or folds
two distinct secondary structures
alpha helix and beta pleated sheet
fibrous proteins
proteins that exhibit either alpha helix or beta-pleated sheets or both
ex. of fibrous proteins
wool, claws, beaks, reptile scales, collagen and ligaments
Q: keratin (human hair) is made up of mostly this protein type
alpha helizs
Q: Silk and spider webs consist of this protein type
beta-pleated sheets
tertiary structure
intricate 3d shape or conformation of a protein that is superimposed on its secondary structure
tert. struc. determines
protein’s specificity
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
quaternary structure
proteins that consist of more than one polypeptide chan
hemoglobin fact about quat. struct
exhibits quat struct. bc it consists of 4 polypeptide chains each forming a heme group
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.
factors affecting protein shape, folding
pH, salt concentration, temp
denaturation
these external factors can affect the weak intramolecular forces causes the protein to lose its shape and thus function this is called denaturation
basic concept of modern bio
protein conformation affects function
chaperone proteins or chaperonins
assist in folding other proteins
prions
accumulations of misfolded proteins in brain cells
diseases caused by prions
Alzheimer’s, Parkinson’s, and mad cow disease
3 complementary techniques used to reveal the 3d shape of proteins
X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and bioinformatics
bioinformatics
uses comps and math modeling to integrate the huge volume of data to predict the 3d model of the structure
2 nucleic acids
RNA and DNA
nucleic acid fuction
encode all hereditary information
Q: info encoded in the sequence of nucleotides in DNA specifies
the amino acid sequences of all proteins
nucleotide consists of
phosphate, 5C sugar (deoxyribose or ribose), and a nitrogen base, (Adenine, Thymine, Cytosine, Guanine, or Uracil)
components of org. mol. that are most involved in chemical reactions
functional groups
how funct. groups are attached
to the C skeleton, replacing one or more H atoms
Amino group
compound name: amino, H-N-H
Carboxyl group
compound name: carboxyl, O–C-OH
Hydroxyl group
compound name: alcohol, OH
Phosphate group
compound name: phosphate, O–P-O-O-O
