Exam 1 Flashcards
Protein Definition
Linear unbranched polymer of 50 or more aminos acids
- amino acids are connected by peptide bonds
- proteins linear seq of amino acids fold to form 3D structure
Nucleic Acid definition
Linear NONbranched polymer of nucleotides
Carbohydrate Definition
an aldehyde or ketone derivative of a polyhydroxyl cpd
-old def: hydrated carbon (CH2O)n
Lipids Definition
Heterogenous group of water insoluble (hydrophobic) organic molecules that can be extracted from tissues by non polar solvents (chloroform)
Protein Functions
ICCE The Muscles Grow
Immune proteins- A highly specific protein-Antibody- detects and removes a foreign substance from cell
Coordinate Motion:
- muscles are made up of mainly proteins
- when muscles contract two proteins slide-actin and myosin
- flagella movement and chromosome movement in mitosis are due to proteins
Control Growth and Differentiation- proteins bind to a specific DNA sequence to express or unexpress another protein
Enzymatic Catalysis- most chemical reactions require enzymes such as globular proteins to increase reactions rate by lowering activation energy
Transport and Storage- small molecules are transported with a cell by transporter proteins
-Hemoglobin carrying oxygen in blood
Mechanical Support- High Tensile strength in bone and skin do to collagen-Fibrous Protein
Generate and Transmission of nerve impulses- sending and receiving signals from nerve cells require a protein that recognizes acetylcholine
Nucleic Acid Functions
Building Blocks of DNA and RNA
- DNA=genetic material
- RNA= adaptor molecule between DNA and protein
Transport chemical Energy storage within the cell
-ATP
Signaling Molecule
-Cyclic AMP
Carbohydrates Function
Energy Source (glucose or sucrose)
Energy Storage (Glycogen in animals and starch in plants)
Structural component (DNA and RNA)
Signaling Molecule
Cell to Cell Recognition (Glycosylation of proteins or other biomolecules)
Glucogenic vs Ketogenic Amino Acids Define
Glucogenic amino acids:
-carbon skeleton converts to Intermediates that can synthesize glucose
Ketogenice amino acids:
- carbon skeleton converts to intermediates (acetyl-CoA or Acetoacetyl-CoA) to form ketone bodies and Fatty acids
- Not substrate of glyconeogenesis
Essential vs Nonessential Amino Acids define
Essential Amino Acids:
- Organism lacks enzymes to synthesize amino acids
- must be obtained from diet
Nonessential amino acids:
-Organism has the enzymes present to synthesize amino acids
Which amino acids are Ketogenic Glucogenic, Both between the nonessential and essential Amino Acids
Essential Amino Acids:
Glucogenic: Val and His Thre Methods
Valine, Histidine, Threonin, Methionine
BOTH: Iley trpd BOTH phesants
Isoleucine, tryptophane, phenylalanine
Ketogenic: KETONES in Leu of Lysine
Leucine, Lysine
NONESSENTIAL AMINO ACIDS Glucogenic: Alanine, Arginine, Asparagine, Aspartic Acid Glycerine, Glutamine, Glutamic Acid Cystein, Serine, Proline
BOTH:
Tyrosine
Ketogenic:
NONE
Which amino acids have dissociable protons and pka values?
Ryan Harris Do You Even Know Connor R-Arginine 12.5 H-Histidine 6.0 D- Aspartic Acid 3.9 Y- Tyrosine 10.9 E- Glutamic Acid 4.3 K- Lysine 10.8 C-Cysteine 8.3
Zwitterion
a molecule containing bot a positive and negative charge on the same molecule
Peptide Bonds
Connect Amino Acids
- Linear, Planar, uncharged
- Fixed due to resonance-has double bond like characteristics
- Trans configuration for carbonyl oxygen and N-H due to steric hindrance
Protein Folding
-due to Change conformation in the N-Calpha and Calpha-C single bonds in the PROTEIN BACKBONE
Phi- angle of rotation of N-Calpha (-80)
Psi- angle of rotation of Calpha-C (+85)
- amino acid sequence contains all the info needed for a protein to fold into 3D structure
- Different secondary structures contain different amounts of amino acids
- “All or none process” due to COOPERATIVE TRANSITION. Rapid transition from folded (native) to unfolded (denatured) state
- Brings amino acids R-groups together at the active sites, R groups come from far and close
Denaturing Protein
- unfolding and disorganization of a protein secondary or tertiary structure
- DOES NOT involve hydrolysis of peptide bond
Denaturing Agents
- Heat
- organic solvents
- Guanidium Chloride
- Urea
- Detergents (SDS)
- Changes in pH (strong acids or bases)
- Heavy Metals (Hg or Pb)
Reducing Agents
-Beta-mercaptoethanol- reduces disulfide bonds
Ramachandran Diagrams
- display favored and disfavored phi or psi bond angles
- many conformations are not allowed due to steric hindrance
- L handed helixes are rare
What are the 4 Levels of protein structure and describe each
Primary
-linear sequence of amino acids
Secondary
- alpha helix, Beta sheets, Beta turns, Omega Loops
- H bonding between carbonyl oxygen and N-H of the BACKBONE
Tertiary
- folding of peptide chains as a result of interactions between R-groups
- Interactions: Disulfide bonds, Hydrophobic interactions, Hydrogen Bonding, Ionic Bonding
- Domains: Units of tertiary Structure-> Helix turn Helix, Helix Loop Helix, Leucine Zipper, Zinc Fingers
Quarternary
-interaction of different polypeptide chains (subunits) to form functional protein
Loops and Turns in Proteins
Connect secondary structures to form Domains of tertiary structures
Beta Turn
-stabilized by H-bonding between Carbonyl Oxygen and N-H bond three amino acids down
-on the surface of proteins
Omega Loops
- Well Defined and rigid
- no repeating structure
- usually on surface of proteins
Alpha Helix
Secondary Structure of Protein
- orientation-Right (clockwise)
- Stabilized by H-bonding between carbonyl oxygen and N-H every fourth amino acid
- 3.6 amino acids per helical turn
- R groups extend outward
Helix is disrupted by:
- Proline
- Large # of charged amino acids
- Bulky side chains (W)
- Branche R groups (V, I)
Proteins that contain Alpha Helixes
Ferritin- Iron storage protein
Hemoglobin- Oxygen carrying protein
Beta Sheets
Secondary structure of protein
- Oreintation- flat, pleated, linear sheets of proteins
- stabilized by H-bonding between carbonyl oxygen and N-H
- amino acids separated by 3.5 A
- can organize into parallel, antiparallel, and mixed
- Beta bends- contain proline and glycine
Proteins that contain Beta Sheets
Fatty Acid binding protein
Green Fluorescent Protein
Alpha Keratin
- Primary component of hair, wool, horns, claws, and hooves
- composed of TWO RIGHT HANDED ALPHA HELIXES intertwined to forma coiled:coiled structure resulting in a L handed helix
- Helixes are cross linked by: Van Der Waals, Ionic Interactins, Disulfide Bonds
- Heptid Repeat
- 3.5 amino acids per turn
- Hair and wool have less disulfide bonds-stretchy
- Horns, claws, and hooves have more disulfide bonds-hard
Collagen
A fibrous protein
- most abundant protein in the human body
- composed of LONG RIGID ALPHA CHAINS wrapped around in a L HANDED TRIPLE HELIX
Triple Helix:
- 1000 amino acids in length
- 3 amino acids per turn
- Repeated Triplet-> Gly-Pro- X
- Proline and Lysine often hydroxylated
- Proline facilitated formation of helix by introducing kink in chain. 100% trans orientation