×
Log in to StudySoup
Get Full Access to OU - CHEM 3653 - Study Guide - Midterm
Join StudySoup for FREE
Get Full Access to OU - CHEM 3653 - Study Guide - Midterm

Already have an account? Login here
×
Reset your password

OU / Chemistry / CHEM 3653 / What type of protein is structural protein?

What type of protein is structural protein?

What type of protein is structural protein?

Description

ul.lst-kix_l3cszzescn3o-6{list-style-type:none}.lst-kix_8oeo8k1lz0d7-4 > li:before{content:"○ "}ul.lst-kix_l3cszzescn3o-5{list-style-type:none}ul.lst-kix_l3cszzescn3o-8{list-style-type:none}.lst-kix_8oeo8k1lz0d7-3 > li:before{content:"● "}.lst-kix_8oeo8k1lz0d7-5 > li:before{content:"■ "}.lst-kix_l3cszzescn3o-7 > li:before{content:"○ "}ul.lst-kix_l3cszzescn3o-7{list-style-type:none}.lst-kix_l3cszzescn3o-8 > li:before{content:"■ "}.lst-kix_8oeo8k1lz0d7-0 > li:before{content:"● "}.lst-kix_8oeo8k1lz0d7-8 > li:before{content:"■ "}.lst-kix_8oeo8k1lz0d7-1 > li:before{content:"○ "}.lst-kix_l3cszzescn3o-3 > li:before{content:"● "}.lst-kix_8oeo8k1lz0d7-2 > li:before{content:"■ "}.lst-kix_l3cszzescn3o-2 > li:before{content:"■ "}.lst-kix_l3cszzescn3o-1 > li:before{content:"○ "}.lst-kix_l3cszzescn3o-0 > li:before{content:"● "}ul.lst-kix_l3cszzescn3o-0{list-style-type:none}.lst-kix_8oeo8k1lz0d7-7 > li:before{content:"○ "}ul.lst-kix_l3cszzescn3o-2{list-style-type:none}.lst-kix_8oeo8k1lz0d7-6 > li:before{content:"● "}ul.lst-kix_l3cszzescn3o-1{list-style-type:none}ul.lst-kix_l3cszzescn3o-4{list-style-type:none}ul.lst-kix_l3cszzescn3o-3{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-4{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-3{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-2{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-1{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-8{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-7{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-6{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-5{list-style-type:none}ul.lst-kix_8oeo8k1lz0d7-0{list-style-type:none}.lst-kix_l3cszzescn3o-4 > li:before{content:"○ "}.lst-kix_l3cszzescn3o-5 > li:before{content:"■ "}.lst-kix_l3cszzescn3o-6 > li:before{content:"● "}

Test 2 STUDY GUIDE

  • Proteins
  • Unique - unique function
  • Nearly all enzymes are proteins
  • Myoglobin and Hemoglobin
  • Globular proteins
  • Structural proteins
  • Collagen
  • Variety of proteins constitute the intracellular scaffolding → cytoskeleton
  • Motor proteins
  • operate along tracks to move cell
  • Myoglobin
  • Relatively small (44 x 44 x 25 Å)
  • Lacks β structure
  • Peptide side chain
  • Iron-containing porphyrin derivative
  • Heme
  • Prosthetic group
  • Heme is wedged in between helices E and F in a hydrophobic pocket
  • Fe ligand by 4 nitrogens and 5th ligand provided by histamine residues
  • Histamine residue of myoglobin
  • His F8
  • 9th residue of F helix
  • Heme is an effective oxygen

  • Oxygen binding equations
  • K = affinity of myoglobin

  • Fractional saturation → Y
  •          → hyperbolic graph
  • → 
  • Structural Proteins
  • Microfilaments (70 Å)
  • Polymers of actin
  • Driven by hydrolysis of ATP

Don't forget about the age old question of What is metaphysical theory?

If you want to learn more check out What is used in the treatment of sewage?
We also discuss several other topics like An attractive “profitable” industry when there is?

  • MicroTubules (240 Å)
  • Polymers of tubulin
  • Driven by hydrolysis of GTP
  • Intermediate filaments (100 Å)
  • Play no part in cell motility
  • No associated motor proteins
  • Keratins
  • Coiled coil
  • 𝛂 (alpha) helices in these residues line up 1 ↔️ 4
  • Collagen
  • Most abundant animal protein
  • 28 types
  • Every 3rd amino acid is gly
  • 30% of remaining are HgP
  • Supportive protein
  • Motor Proteins
  • Myosin
  • 2 heads long tail
  • 20 different types
  • Neck consists of 𝛂 (alpha) helix about 100 Å long
  • Tail is coiled coil
  • Head includes binding site for adenine nucleotide
  • Thick filaments
  • Tails associate so heads stick out
  • Thin filaments
  • Consist of actin filaments and actin binding proteins
  • Kinesin
  • Microtubule - associated motor protein
  • Large protein
  • Globular heads
  • Coiled coil tails
  • Head
  • 100 Å lon
  • Consist of an 8 stranded β sheets flanked by 3 𝛂 (alpha) helices on each side
  • Tubulin binding site and nucleotide binding site
  • Moves cargo to (t) end of microtubule

If you want to learn more check out What are the different kinds of construct validity?

We also discuss several other topics like What is a change in the allele frequencies in a population - evolution doesn’t involve changing the genetics or physical features of individuals?

We also discuss several other topics like What are the different kinds of effectors?

  • Enzymes
  • In vitro
  • Under physiological conditions
  • Peptide bond that links amino acids has a half life of 20 years
  • Broken down by hydrolysis
  • Long half life is advantageous
  • An enzyme is a catalyst that speeds up the half life of the peptide bond
  • Most are proteins
  • Few are made with RNA (ribozymes)
  • Best studied enzyme is chymotrypsin
  • Digestive protein synthesized in the pancreas → secreted in small intestine and there breaks down dietary proteins
  • 241 amino acid residues form compact 2 domain structure
  • Active site
  • Where hydrolysis of a peptide occurs
  • Reaction specificity
  • Most enzymes are highly specific for their reactants and products
  • Types of Enzymes - Functions
  • Oxidoreductases
  • Oxidation- reduction reactions
  • Transferases
  • Transfer of functional groups
  • Hydrolases
  • Hydrolysis reactions
  • Lyases
  • Group eliminations to form double bonds
  • Isomers
  • Isomerization reaction
  • Ligases
  • Bond formation or ATP hydrolysis
  • Isozymes
  • Multiple enzymes catalyzing the same reaction
  • Differ in catalytic properties
  • Stabilize the transition state
  • Increase the reaction rate
  • Increase reaction rate by bringing reactant groups closer together thus increasing the collisions
  • Proximity and orientation effects explain some of the residual activity of the chymotrypsin


  • The progress of the concentration change can be shown as velocity (v)
  • ; [s] = [substrate] ; [P] = [product]
  • The more catalyst present the faster
  • Linear
  • When hyperbolic
  • Suggests that an enzyme physically combines with the substrate.
  • Increases at first almost linearly then as more substrate is added, enzyme activity increases less
  • Michaelis-Menton Equation
  • Unimolecular
  • First order
  • ; K = rate constant → units s-1

Page Expired
5off
It looks like your free minutes have expired! Lucky for you we have all the content you need, just sign up here