-
What is a glycosidic linkage?
Covalent bond formed by condensation reactions joining monosaccharides
-
What are the 4 main types of glycosidic linkages?
-
What are 2 most common disaccharides w/their linkage types?
- Sucrose α-1,2
- Lactose β-1,4
-
Humans can break down maltose but not cellobiose b/c. . . .
Shape differences causing changes in biological nature
-
What are oligosaccharides?
Chain of 3-20 monosaccharides
-
What are polysaccharides?
Giant chains of monosaccharides connected by glycosidic linkages
-
Polysaccharides are primarily used for ___ & ___ in the body.
Storage & structural support
-
Starch & glycogen are made up of what?
Repeating monomers of glucose
-
Galactosamine is a major component of ___.
Cartilage
-
Glucosamine is a component of ___ & found where?
Chitin in skeletons of insects, prawns, crabs & cell walls of fungi
-
What makes lipids hydrophobic?
Non polar covalent bonds between hydrogen & carbon
-
What causes lipids to want to stick to each other?
Van der Waals forces
-
Lipids in cell membrane structure are known as ____.
Phospholipids
-
Carotinoids are lipids that do what?
Capture light energy in the eyes
-
The polymer triglyceride is composed of what?
4 monomers - 3 fatty acids & 1 glycerol molecule
-
What bonds are used to link lipid molecules together?
Ester Linkages formed by condensation reactions
-
What comprises a fatty acid?
Long chain of hydrocarbons w/carboxyl grp at one end
-
When speaking of a saturated fat; what does saturated mean?
It means the hydrocarbon chain in saturated w/hydrogen
-
T or F. . Animal fats & tropical plant oils are saturated?
True
-
What tells us that a fatty acid is unsaturated?
- At least 1 double bonded carbon causing bends in the chain
- Liquid at rm temp
-
How are hydrogenated oils created?
By adding hydrogen to unsaturated fats.
-
What is the structure of a phospholipid?
- 2 hydrophobic fatty acid tails
- 1 hydrophilic phosphate attached to the glycerol
-
In an aqueous environment, how are phospholipids oriented & what do they form?
- Phosphate heads face outward & fatty acid tails inward (tail to tail)
- Cell membranes
-
What is β-carotene used for in plants? In animals?
- Trap light in photosynthesis
- 2 identical pieces of vitamin A required for vision
-
What is the mother structure for steroid hormones?
cholesterol
-
What vitamins are fat soluble?
A,D,E & K
-
Define Nucleic Acids.
Polymers specialized for storage, transmission & use of genetic info
-
What is the monomer of a nucleic acid?
Nucleotide
-
What are the 3 components of nucleotide?
- Pentose Sugar
- Phosphate grp
- Nitrogen containing base
-
What are the 2 sugars that could be in a nucleotide?
-
What is the difference between ribose & deoxyribose?
An O molecule at Carbon #2
-
Waxes protect against ___ in ___, ___ & ___ ___.
- dehydration
- Hair, feathers, insect eggs
-
What is vitamin A mad fr & used for?
- β-carotene
- Norm development, Maintenance of cells & night vision
-
Vitamin D is made in the ___ fr exposure to ____.
-
Vitamin D does what?
Aids absorption of Ca & important for bone health
-
Vitamin E is a good ___.
Antioxidant
-
Vitamin K is important for ___ ___.
Blood Clotting
-
Nitrogenous bases can be either ___ or ___ in structure.
- Pyrimidine - single ring structure
- Purine - fused double ring structure
-
Covalent bonds between nucleotides are called ___ ___.
Phosphodiester Linkages
-
Describe the phosphodiester linkage.
Phosphate grp bonds to #3 C of 1 pentose & #5 C of another
-
RNA molecules consist of what?
- Single strand of nucleotides
- Unpaired bases
-
DNA is a ___ ___ of nucleotides.
Double strand
-
The double stranded DNA is antiparallel which means?
One strand ends w/free C 5' of deoxyribose & other ends w/ C 3' of deoxyribose
-
What are the 4 bases found in DNA?
- Adenine (A) purine
- Guanine (G) purine
- Thymine (T) pyrimidines
- Cytosine (C) pyrimidines
-
What are the 4 main types of Biomolecules (macromolecules)?
- Proteins
- Carbohydrates
- Lipids
- Nucleic Acids
-
What are some roles of lipids (2)?
- Energy Storage
- Structural support
-
What are some roles of proteins (8)?
- Structural support (collagen)
- Catalysis (enzymes)
- Transport (hemoglobin)
- Protection & defense (Antibodies/keritin)
- Regulation of metabolic activities
- Maintenance of Homeostasis
- Info Storage
- Means for mvmt, growth & development
-
What are 2 roles of carbohydrates?
- Energy Storage (glycogen)
- Mvmt, growth & development
-
What are polymers?
Long chains of monomers linked together by covalent bonds
-
___, ___ & ___ are considered lg molecules.
Proteins, Polysaccharides & Nucleic acids
-
What 6 elements compose monomers?
C, H, O, N, P, S
-
___ & ___ make up skeletons & then special grps of atoms attach in specific places.
Carbons & Hydrogens
-
What are functional groups?
Special grps of atoms w/specific chem properties that attach to a larger molecule
-
An isomer is what?
- Molecule w/same chem formula but atoms arranged differently
- ie glucose & fructose
-
Explain structural Isomers.
Isomers that differ in how their atoms are joined together or bonding arrangement
-
Explain geometric Isomers.
Isomers that differ in the placement of their functional grps or atoms around a double bond
-
Each functional grp has a ___ ___ ___ which it confers to the larger molecule.
Specific Chem Property
-
Optical or stereoisomers occur when . . . .
An α-carbon has 4 different functional grps attached to it & 2 resulting molecules are mirror images of each other.
-
What does a condensation or dehydration reaction do?
Builds polymers fr monomers by covalently bonding OH grp of 1 to a H of another w/release of a molecule of H₂O
-
What 2 things are required for a condensation reaction?
Energy & special enzymes
-
What does a hydrolysis reaction accomplish?
Breaks covalently bonded polymers into monomers w/the addition of H₂O
-
What are 3 characteristics of hydrolysis reactions?
- H₂O reacts w/covalent bonds linking polymers together
- Energy is released
- Performed by enzymes
-
What is the monomer or building block in a protein?
Amino Acids
-
Explain a peptide bond?
Covalent bond between amino acids formed by a condensation reaction between a carboxyl grp & amino grp of another resulting in a polypeptide.
-
What is a polypeptide?
Single chain of amino acids held together by peptide bonds
-
What are the 3 parts of an amino acid structure?
- Amino Grp - N containing portion
- Acid - Carboxyl Grp
- R-Grp - Functional grp attached to α-carbon
-
Explain the R-Group.
- Functional Group attached to α-carbon
- Makes 1 type of amino acid different fr another
-
Explain a Zwitterion.
- At pH of 7, both amino & carboxyl group are ionized
- Carboxyl grp lost an H ion & amino grp has gained 1
-
Explain why we have D-amino acids & L-amino acids.
B/c α-carbon has 4 different functional grps attached to it we can get 2 isomeric forms that are mirror images. One is D-form & other is L-form.
-
What is the exception to the α-carbon rule & why?
Glycine b/c it has a H in its R group
-
If we shine light at a D-amino acid what happens & what does D stand for?
- Light will rotate clockwise
- D means dexterrotatory
-
If we shine light at an L amino acid what happens & what does L stand for?
- Light will rotate counterclockwise
- L stands for levorotatory
-
Only ___ ___ are commonly found in the proteins of most organisms.
L-amino acids
-
What are the 3 primary classifications of amino acids?
- Charged R-Grps
- Polar w/o a charge
- Non-polar hydrophobic
-
What are the 3 special cases of amino acids?
-
The 1st amino acid of a peptide is called the what?
- N-terminus amino acid
- Free amino grp
-
The last amino acid of a peptide is called the ___ ___ ___.
- C-terminus amino acid
- Free carboxyl grp
-
What are the 4 levels of protein structure?
- Primary
- Secondary
- Tertiary
- Quaternary
-
The primary structure of a protein is its ___ ___ ___.
Amino acid sequence
-
The secondary structure of a protein requires ___ ___.
hydrogen bonding
-
What are the 2 common secondary structures?
- α helix - single poly peptide chain
- β pleated sheet - single or multiple polypeptide chains
-
Explain α helix structure.
Right handed coil w/spiral shape being caused by H bonds between slightly pos H & slightly neg O
-
What could prevent the creation of the α helix structure?
Large R groups
-
Explain a β sheet.
Sheet like structure stabilized by H bonds between regions of a peptide
-
Explain Parallel β sheets.
- Sheets where strings of peptides are aligned all the same way.
- Carboxyl grps on 1 end & amino grps on the other
-
Explain Antiparallel β sheets.
- Sheets where strings of peptides are aligned in an alternating pattern.
- 1st string starts w/carboxyl grp then 2nd starts w/amino & so forth
-
How is the tertiary structure of a protein formed & what determines its shape?
- By bending & folding secondary structures
- Determined by interaction between R groups
-
How can R groups interact in tertiary structures?
- Form disulfide bridges
- Hydrogen bonding
- Van der Waals forces
- Salt bridges
- Hydrophobic Interactions
-
What are salt bridges?
Ionic interactions between pos & neg charges deep in protein
-
What is a quaternary structure?
- Subunits of tertiary structures coming together to form final protein.
- ie hemoglobin
-
What are chaperonins?
Specialized proteins that keep other proteins fr interacting inappropriately w/one another prior to positioning
-
When proteins misfold what could happen?
They don't interact properly w/the environment & build up. The body tries to get rid of them & creates more problems in so doing
-
What are some reasons for protein specificity (5)?
- Cells can attach together by protruding proteins
- Enzymes need certain shapes to bind correctly
- Carrier proteins allow substances to enter cell
- Chem signals (ie hormones) bind to proteins on cell surface
- Antibodies recognize virus shape & bind to it
-
What is denaturation?
- Loss of protein's normal 3-D structure
- Only primary structure remains intact
- Can be reversible or irreversibl
- ie cooking an egg
-
What can cause denaturation?
- Changes in temp or pH
- High concentrations of polar substances
-
T or F: Some proteins can resist denaturation & be boiled for days bt once they cool they retain their reg activity
True
-
What's are 2 proteins that resist denaturation/
-
What is the issue w/proteins that resist denaturation?
- They remain present even when we think they have been eliminated.
- ie on surgical instruments
-
What does a carbohydrate contain?
Carbon molecules w/hydrogen & hydroxyl groups
-
How do carbs act as energy storage molecules in plants? In animals?
- Plants produce & store as sugar & starches
- Animals store as glycogen
-
What are the 4 major categories of carbohydrates?
- Monosaccharides
- Disaccharides
- Oligosaccharides
- Polysaccharides
-
What is the general formula for a carb monomer & in what ratio?
-
What is the most common monosaccharide & its formula?
-
When bonding monosaccharides what must we remember?
- H₂O is released therefore it comes out of the disaccharide
- C₆H₁₂O₆ + C₆H₁₂O₆ --> C₁₂H₂₂O₁₁ + H₂O
-
Like proteins, monosaccharides are also stereoisomers. Which series (d or L) are most common?
d-series
-
Isomers of glucose are known as ___ & come in what forms?
- Anomers
- β-glucose or α-glucose
-
What distinguishes α-glucose fr β-glucose?
α-glucose has H on top @ C#1; β it is on bottom
-
A hexose is a ___ ___ sugar.
6 carbon
-
A 5 carbon sugar is called ___ & found in ____.
|
|
