Ch 1 - Bio Chemistry Flashcards
What elements do Carbohydrates and proteins have in common?
What element separates out proteins from carbs?
C H N O
C H N O S - Sulfur
What are the polysacharrides of starch
amylose - 1-4 glycosidic linkages of Glucose
amylopectin - 1-4 glycosidic linkages and 1-6 glycosidic linkages (Like Glycogen but less branched)
What is a nucleon?
Proton or Neutron
Are soluble protein’s electrostatic interactions stronger internally or externally?
Internally - The water hydrogen bonds create an solvent shell that weaken the electrostatic interactions
-ΔG means?
Spontaneous reaction (exergonic)
+ΔG means?
Non-Spontaneous reaction (endergonic)
ΔG = 0 means?
The reaction is at equilibrium
Are almost all exothermic reactions spontaneous or non-spontaneous?
Spontaneous
-ΔH and +ΔS means what?
The reaction will be spontaneous regardless of temperature
ΔG = ΔH - T ΔS
Open System
mass and energy can exchange
Closed System
allows energy to transfer, but not mass
Isolated System
Neither energy nor mass can transfer
Chemotroph
Derive free energy from the oxidation of fuel molecules
Biotin
Biotin is a cofactor involved in carboxylation and decarboxylation reactions.
Transfers CO2
Used in Glycolysis
S-Adenosylmethionine (SAM)
CoFactor involved in CH3 (methyl) group transfers
Explain steric hinderance in Peptide bonds and why it’s significant
The bond has about a 40% double bond characteristic and takes on a trans formation. This makes it so the peptide bond is rigid.
How man structural isomers would there be for
- Val
- Tyr
- Ala?
3! = 321 = 6
How man optical isomers would there be for ValTyrAla?
N = 3 since each is chiral 2^3 = 8
What are the primary, secondary, tertiary, and quaternary structures of proteins?
primary: sequence of amino acids held by covalent bonds. This includes the peptide bond and disulfide bond.
secondary: This is the 3D conformation of localized regions caused by hydrogen bonds. (Beta sheets)
tertiary: This is the 3D structure of the entire protein held together by hydrogen bond, disulfide bonds, salt bridges (electrostatic interactions), and van der walls interactions.
quaternary: How different peptide chains interact with all the same interactions as tertiary
What is the difference between digestion and denaturing
Digestion breaks the primary structure, denaturing only breaks the secondary -> quaternary
How does heat work as a denaturing agent?
It breaks Hydrogen bonds. It causes the molecules to vibrate too violently.
How does radiation work as a denaturing agent?
It breaks Hydrogen bonds. It causes the molecules to vibrate too violently.
How do detergents work as a denaturing agent?
affects salt bridges and H bonds
How do acids / bases work as a denaturing agent?
affects salt bridges and H bonds
How do salts of Heavy Metals such as Ag+, Hg++, and Pb++ work as a denaturing agent?
Bond with SH groups to form precipates as well as acidic amino acids
How does Urea work as a denaturing agent?
Disrupts hydrogen bond.
How many hydrogen bonds do the nucleotides A-T or A-U have?
2
How many hydrogen bonds do the nucleotides G-C have?
3
What’s the difference between a nucleotide and a nucleoside
A nucleoside is a sugar and N-base. A nucleotide has a phosphate group attached as well on the 5’ OH
What makes up the backbone of DNA?
The sugar-phosphate complex. The nitrogenous bases make up the middle of DNA.
Phosphodiester bonds between 5’ and 3’ OH on Glucose
How are DNA monomers linked?
Phosphodiester bonds between the 5’OH of one nucelotide and the 3’ OH of another.
