Term
|
Definition
Proline
(Pro)
P
Special Case |
|
|
Term
|
Definition
Glycine
(Gly)
G
Special Case |
|
|
Term
|
Definition
Cysteine
Cys
C
Special Case |
|
|
Term
|
Definition
Selenocysteine
(Sec)
U
Special Case |
|
|
Term
|
Definition
Glutamine
(Gln)
Q
Polar Uncharged Side Chain |
|
|
Term
|
Definition
Asparagine
(Asn)
N
Polar Uncharged |
|
|
Term
|
Definition
Threonine
(Thr)
T
Polar Uncharged |
|
|
Term
|
Definition
Serine
(Ser)
S
Polar Uncharged |
|
|
Term
|
Definition
Glutamic acid
(Glu)
E
Negative |
|
|
Term
|
Definition
Aspartic Acid
(Asp)
D
Negative |
|
|
Term
|
Definition
|
|
Term
|
Definition
Histidine
(His)
H
Postive |
|
|
Term
|
Definition
Arginine
(Arg)
R
Postiive |
|
|
Term
|
Definition
Alanine
(Ala)
A
Hydrophobic |
|
|
Term
|
Definition
Valine
(Val)
V
Hydrophobic |
|
|
Term
|
Definition
Isoleucine
(Ile)
I
Hydrophobic |
|
|
Term
|
Definition
Leucine
(Leu)
L
Hydrophobic |
|
|
Term
|
Definition
Methionine
(Met)
M
Hydrophobic |
|
|
Term
|
Definition
Phenylanlinine
(Phe)
F
Hydrophobic |
|
|
Term
|
Definition
Tyrosine
(Tyr)
Y
Hydrophobic |
|
|
Term
|
Definition
Tryptophan
(Trp)
W
Hydrophobic |
|
|
Term
4 Classes of Biomolecules
Chap. 1 |
|
Definition
| 1. Lipids 2. Carbohydrates 3. Proteins 4. Nucleic Acid |
|
|
Term
|
Definition
20 Amino Acid
Folds into 3D Shape
4 functions= structure, motility, signaling, catalyst |
|
|
Term
|
Definition
Information molecule
Pyrmidine= thymine, cytoseine, uracil
Purine= Guanine, adenine |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
4 Levels Cellular Organization
Chap. 1 |
|
Definition
Level 1: Monomeric units (Nucleotide, Sugars, amino Acid)
Level 2: Macromolecules (DNA, Proteins, Cellulose)
Level 3: Supramolecular Complexes (Chromatin, plasma membrane, cell wall)
Level 4: Organelles. |
|
|
Term
|
Definition
same
atoms,
same
chemical
bonds,
different
arrangement
of
atoms. |
|
|
Term
Chiral Vs. Achiral
Chap. 1 |
|
Definition
Chiral= mirror image cannot be superimposed
Achiral= mirror image can be superimposed |
|
|
Term
Free energy change
Chap. 1 |
|
Definition
ΔG =ΔHsystem-‐TΔSsystem
When ΔG is negative, a process is
spontaneous (exergonic))
When ΔG is positive, a process is
nonspontaneous(endergonic). |
|
|
Term
The Equilibrium Constant
Chap. 1 |
|
Definition
|
|
Term
Relationship between Q & K & ΔG
Chap. 1 |
|
Definition
Q=[C]c[D]d
[A]a[B]b
ΔG = 0 or Q=K,the system is at
equilibrium. |
|
|
Term
Free energy and Equilibrium
chap. 1 |
|
Definition
ΔG° = -RT ln K
or
K = e-ΔG°/RT |
|
|
Term
Metabolic reactions
Chap. 1 |
|
Definition
| Catabolic (degrade) & Anabolic (build) |
|
|
Term
|
Definition
|
|
Term
Types of intermolecular interactions
Chap. 2 |
|
Definition
|
|
Term
Noncovalent interactions
Chap.2 |
|
Definition
| stabilization of proteins and nucleic acid. Bind reactants to enzyme |
|
|
Term
|
Definition
|
|
Term
Henderson Hasselbach Equation
Chap. 2 |
|
Definition
pH in relationship to acid/base.
pH =pKa+log[A-]
[HA] |
|
|
Term
|
Definition
PI= (Pka1+Pka2)/2
Use 2 pkas around neutral atom |
|
|
Term
|
Definition
| joins amino acids amine group left to carboxyl right side of peptide. Molecules named by amino acid with -yl suffix |
|
|
Term
Ion Exchange chromatography
Chap. 3 |
|
Definition
| exploits differences in charge and magnitude at given pH |
|
|
Term
Size-exclusion chromatography
Chap. 3 |
|
Definition
| separates proteins according to size. |
|
|
Term
Affinity Chromatography
Chap. 3 |
|
Definition
| separates proteins by binding specificity. |
|
|
Term
|
Definition
| Separates proteins with an applied electrical field. |
|
|
Term
Protein structures
Chap. 3 |
|
Definition
| 1. AA sequence 2. Arrangement of AA (Alpha helix) 3. interaction between peptides 4. polypeptide folding |
|
|
Term
molecular mass of proteins
Chap. 3 |
|
Definition
| each AA has a mass of 110g/mol or Daltons |
|
|
Term
|
Definition
| long fibers. Two alpha helices form coiled coil. |
|
|
Term
|
Definition
| 3 left hand helices coiled around each other. |
|
|
Term
|
Definition
| store O2 to RBC and release to rest of the body. Contains prosthetic Heme group. |
|
|
Term
Positive Cooperativity
Chap. 5 |
|
Definition
| Heme increases affinity for O2 as more O2 molecules bind. Due to quaternary structure. |
|
|
Term
Cooperative O2 binding
Chap. 5 |
|
Definition
Deoxyhemoglobin= T-State
Oxyhemoglobin= R-state.
Dimers Rotate 15* |
|
|
Term
|
Definition
| Acidic conditions decrease affinity for O2 in hemoglobin driving an exchange at the tissue. |
|
|
Term
|
Definition
| stabilizes Deoxyhemoglobin in low O2 environments. |
|
|
Term
Sickle Cell Anemia
Chap. 5 |
|
Definition
| Results from switch of Glu-6 to Val-6 of Beta chain. Results in unusual hydrophobic interactions. |
|
|
Term
Allosteric Protein
Chap. 5 |
|
Definition
| binding of a ligand that affects the binding ability of another protein. |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
properties of thermodynamic reactions
Chap. 5 |
|
Definition
The free energy (DG) of the reaction: the free energy difference between the reactants and the products.
activation energy: the energy required to initiate the conversion of reactants into products |
|
|
Term
thermodynamic landscape
Chap. 5 |
|
Definition
|
|
Term
|
Definition
|
|
Term
Michaelis constant
Chap. 6 |
|
Definition
Km = k-1 + k2
k1
k1=E+S-->ES K-1= ES-->E+S K2=ES-->E+P |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
Km = rate of ES breakdown
rate of ES formation |
|
|
Term
|
Definition
|
|
Term
3 types of inhibition
Chap. 6 |
|
Definition
Competitive: I binds to E only
Uncompetitive: I binds to ES only
Mixed: I binds to E or ES |
|
|
Term
Competitive inhibition
Chap. 6 |
|
Definition
|
|
Term
|
Definition
|
|
Term
| Slope related to lineweaver |
|
Definition
|
|
