Week 4 Flashcards
__________ __________ is the form of OMT in which patient’s muscles are actively used on request, forma precisely controlled position, in a specific direction, and against a distinctly executed physician counterforce
Muscle Energry
List 3 techniquest that involve patients active cooperation in muscle energy:
1.) Contract a muscle/muscles
2.) Inhale or exhale
3.) Move one bone of a joint in a specific direction relative to the adjacent bone
For example, if using a technique that begins in the position of ease and transitions to position of restriction, is this indirect or direct osteopathic tx?
Since STARTING at position of EASE, this is INDIRECT tx
Ex: if performing treatment that starts by engaging the restrictive barrier and moves towards position of ease, is this indirect or direct osteopathic treatment?
Direct
Define: concentric contraction
Contraction of a muscle resulting in the approximation of the origin and insertion
Define: concentric
Contraction of a muscle resulting in the approximation of the origin and insertion
_____________ _________ of a muscle resulting in the approximation of the origin and insertion. i.e. elbow flexion phase of bicep curls
Concentric contraction
Define Eccentric contraction
The muscle tension allow the origin and insertion to separate, in effect to lengthen
______________ _____________ is the muscle tension which allows the origin and insertion to separate, in effect to lengthen. i.e. elbow extension phase of bicep curls
Eccentric contrcation
Define: isolytic contraction
When external forces overcome the muscle contraction, causing muscle lengthening
___________ ___________ is when external forces overcome the muscle contraction, causing muscle lengthening
Isolytic contraction
___________ ____________ is when muscle tone stays the same but the length of the muscle changes
Isotonic
Define: isotonic contraction
When muscle tone stays the same but the length of the muscle changes
Define: isometric contraction
Distance between the origin and the insertion of the muscle is maintained at constant length
What is the difference between the binding site and catalytic site of an enzyme?
- Binding site is the area that holds the substrate in proper place
- Catalytic site is where the actual reaction occurs
What is the active site on an enzyme?
2 component pocket of an enzyme, is composed of the binding site and catalytic site
What is the difference between a cofactor and coenzyme?
- Cofactor is an inorganic
- Coenzyme is a nonprotein organic component needed for enzyme function
What is a Holoenzyme?
The protein plus its cofactor or coenzyme?
A __________________________ is an enzyme protein plus it cofactor/coenzyme
Holoenzyme
A ________________________ is an enzyme protein without its cofactor/coenzyme
Apoenzyme
What is an apoenzyme?
Enzyme protein without its cofactor/coenzyme
What is an example of a prosthetic group?
Heme
_______________ ______________ a component that’s very tightly (covalently or non-covalently) attached to the protein. It can be inorganic (metal ions), organic (vitamin B1, B2, B3 and so on) or mixed.
Prosthetic group
What is a prosthetic group?
a component that’s very tightly (covalently or non-covalently) attached to the protein. It can be inorganic (metal ions), organic (vitamin B1, B2, B3 and so on) or mixed.
What do enzymes do to a reaction?
- LOWERS THE ENERGY OF ACTIVATION
- it lowers the amount of energy needed for the reaction to take place
What is ΔG in an enzyme reaction?
- the free energy of the overall reaction
How can you calculate the free energy of a reaction?
Energy of reactants minus the energy of the products
What does an enzyme do to its substrate?
- Stabilizes the transition state
- By stabilizing the transition state the enzyme increases the concentration of the reactive intermediate that can be converted to product
List 5 factors that can affect reaction velocity
- Substrate concentration
- Temperature
- pH
- Cofactors
- Coenzymes
Enzymes following Michaelis-Menten kinetics show a ___________________ curve.
Hyperbolic
Allosteric enzymes show a ____________ curve.
Sigmoidal curve
_________________ ____________________ increases with substrate concentration until a maximum _____________________ is reached.
Reaction velocity
velocity
On an enzyme kinetics graph, what does the linear phase of a reaction equate to?
It is the change in reactant or product concentration as soon as enzyme and substrate are mixed.
Describe the model of Michaelis Menten Kinetics
the enzyme reversibly combines with its substrate to form an ES complex that subsequently breaks down to product, regenerating the free enzyme
The Michaelis-Menten equation says Vo =
Vmax [S] / Km + [S]
What is Km in enzyme kinetics?
- Km is the [SUBSTRATE CONCENTRATION] where velocity of the reaction is 1/2 Vmax
What does small Km reflect?
- Small Km indicates HIGH affinity of the enzyme for substrate because Vmax is reached at a sooner point
When [S] is much less than Km, the velocity of the reaction is approximately proportional to the substrate concentration which is what order of rate kinetics?
First order
Describe first order enzyme kinetics
At low concentrations of substrate where [S] < Km, the velocity of the reaction is proportional to substrate concentration
When [S] > Km, the velocity of the reaction is _________________ order, meaning the velocity is constant and independent of substrate concentration.
Zero order
Describe zero order enzyme kinetics
When [S] > Km, the velocity is almost constant and independent of substrate concentration
What does the Y intercept represent on a Lineweaver-Burk analysis?
1/ V max
What does the slope of a Lineweaver Burk analysis represent?
Km / Vmax
What does the X intercept represent on a Lineweaver Burk analysis?
1/[S]
What types of bonds do reversible enzyme inhibition form?
Inhibitor forms noncovalent bonds that readily dissociate from an enzyme
What types of bonds are formed between inhibitor and enzyme in Reversible inhibition?
What about in irreversible inhibition?
Reversible: noncovalent bonds
Irreversible: covalent bonds
In _______________________ inhibition the enzyme is only inactive when the inhibitor is present
Reversible
Where is the site of attack in irreversible inhibition?
the amino acid group that participates in the normal enzymatic reaction
What are Km and Vmax in competitive inhibition?
- Km is decreased because the affinity for the substrate is decreased
- Vmax stays the same
Vmax is directly proportional to:
The number of enzymes available
In enzyme inhibition, Vmax reduces in all types EXCEPT:
Why?
V max does not change in Competitive inhibition because can add more substrate
What are Km and Vmax in noncompetitive inhibition?
- Vmax lowered
- Km unchanged because the substrate still binds to the enzyme and the inhibitor is bound to the allosteric site
What are Km and Vmax in uncompetitive inhibition?
- Vmax lowered
- Km LOWERED, because the allosteric inhibitor disallows the enzyme/substrate to disassociate which raises their affinity for one another
___________ ____ ___ is what type of inhibitor of citrate Synthase
- Succinyl CoA
- Uncompetitive
What are three examples of covalent modification as a form on enzyme regulation?
- Phosphorylation
- ADP Ribosylation
- Methylation
What is sequestration as a form of enzyme regulation?
The enzyme is taken away and not available for substrate use
What are induction and repression as forms of enzyme regulation?
Is this a fast or slow change? Why?
- Increase or decrease gene expression such that it increases or decreases the amount of enzyme
- Slow as in hours to days due to delays of expression
- Examples of covalent modification as a form of enzyme regulation, include phosphorylation and ADP ribosylation. The action is completed by:
- Impacts _______ and/or ______
- Time required for change: immediate to minutes
- Another enzyme
- Change in Vmax and/or Km
Converting a zymogen to its activated form is what type of enzyme regulation?
Proteolytic cleavage
Phosphorylation as a type of covalent enzyme modification will act on what 3 AA?
Ser
Thr
Tyr
ADP ribosylation as a type of covalent enzyme modification will normally act on what Amino acid?
Arg
Methylation as a form of covalent enzyme modification will normal act on what amino acids?
Lys
Arg
_____________________ is a type of covalent enzyme modification that acts on the amino acids: Ser, Thr, and Tyr. What are three examples?
- Phosphorylation
2a. GS
2b. GP
2c. PK
____-_______________________ is a form of covalent enzyme modification that acts on Arg. What are two examples of this?
- ADP-Ribosylation
2a. G proteins
2b. eEF-2
_______________________ is a form of covalent enzyme modification that acts on Lysine and Arg. What is an example of this type of modification?
Methylation
Histone
Phosphorylation as a form of enzyme regulation occurs at Serine, Threonine and tyrosine, why?
What enzymes normally catalyze this reaction?
What enzyme can reverse this reaction?
- They have -OH groups in their side chain
- Protein kinases
- Protein phosphatases
The enzyme, ART initiates ADP-ribosylation on Arginine. The enzyme ARH removes the ribose nucleotide from Arg. What two clinical correlations does this relate to?
- Cholera
- Pertussis
Cholera is a bacterial infection of the small intestine by the bacterium Vibro cholerae. The classic symptom is watery diarrhea. What is the toxin doing on the cellular level?
Cholera toxin ADP-ribosylates the G protein Gαi
- Covalent enzyme regulation
Infection by the bacterium Bordetella pertussis is a form of covalent enzyme modification. What is occurring on the cellular level?
Pertussis toxin ADP-ribosylates G protein Gαi
Allosteric regulation occurs in allosteric enzymes. Why?
Because allosteric enzymes have two or more subunits and active sites
Allosteric enzymes exhibit cooperativity. How does substrate concentration impact their kinetics?
These enzymes are regulated by:
At high [S], more enzymes are found in the R state
- regulated by effectors
- Describe the displacement of the curve for allosteric enzyme kinetics for POSITIVE EFFECTORS
- Describe the displacement of the curve for allosteric enzyme kinetics for NEGATIVE EFFECTORS
- positive effectors will stabilize the relaxed from and curve will shift left, indicating less [S] needed to reach V max
- Negative effectors: stabilize the Tense form and curve will shift right indicating need for more substrate to achieve V max
Enzyme nomenclature:
EC 1
What does this enzyme do?
- Oxidoreductase
- Loss of H+ and electron
Enzyme nomenclature:
EC 2
What does this enzyme do?
- Transferases
- Transfer group(s) containing C-, N-, or P-
Enzyme nomenclature:
EC 3
What does this enzyme do?
- Hydrolase
- Break substrate using H2O
Enzyme nomenclature:
EC 4
What does this enzyme do?
- Lyases
- Catalyze cleave of C-C or C-S bonds and certain C-N bonds
Enzyme nomenclature:
EC 5
What does this enzyme do?
- Isomerases
- Relocates a group within the SAME molecules
Enzyme nomenclature:
EC 6
What does this enzyme do?
- Ligases
- Formation of bonds b/t Carbon & -N, -O, -S
Peptide bonds are between what terminus of Amino acids?
B/t Carboxyl terminus and Amino terminus
What direction are peptide bonds read and written?
N terminus to C terminus
What type of bonds are key in stabilizing secondary protein structures?
Hydrogen bonds between the carbonyl oxygen from one amino acid to an α nitrogen of a distant amino acid
What two amino acids disrupt α helix? Why is this the case?
- Proline and Glycine
- They have no side chain
β sheets involve peptides side by side in a parallel or antiparallel orientation. How can you discern their direction?
Are the N terminus of the chain on the SAME SIDE OR OPPOSITE SIDE ?
Opposite = ANTIPARALLEL
Same sided = PARALLEL
Amyloid deposits in the brain make ____-______________ more likely to aggregate and implicated in Alzheimer’s disease
β pleated sheets
________________________ disease is caused by protein aggregation through β pleated sheets; aggregation of polyglutamine β-strands of the __________________ protein
- Huntington
- Huntingtin
How do amyloid plaques form in Alzheimer’s disease?
Aggregation of amyloid β, a peptide derived from amyloid precursor protein through sequential cleave by β-secretase and γ-secretase
What causes Creutzfeldt-Jakob disease?
Prion protein in a misfolded form by inducing the formation of an amyloid fold
What creates the turns in β pleated sheets?
Amino acids Proline and Glycine
What are Porins/what do they do?
Proteins found on outer-membrane of Gram - and Gram+ bacteria. They transport molecules across the membrane and act as a channel
Mutations in porin protein contribute to ABX resistance
List 4 forces involved in maintaining tertiary structure
Hydrogen bonds
Disulfide bonds
Hydrophobic interactions
Electrostatic interactions
Electrostatic interactions are synonymous to:
Ionic interactions and dipole dipole interactions
After tertiary structures are denatured they cannot revert to their original tertiary structure with the exception:
Ribonuclease which can refold on its own
What hold quaternary protein structures together?
Noncovalent interactions
- Hydrogen bonds
- Hydrophobic interactions
- Electrostatic interactions
In Sickle Cell disease what two Amino Acids are involved?
Glutamic acid is replaced with nonpolar Valine
What structure in the axilla divides the Axillary artery into three parts?
Pectoralis minor
- The lateral border of the 1st rib and the medial border of pectoralis minor is what portion of the axillary artery?
- What branches come off the artery?
1.) 1st division of the axillary artery
2.) Superior thoracic artery
1.) The portion of the axillary artery that passes beneath the pectoralis minor is:
2.) What branches off this artery?
1.) 2nd division of the axillary artery
2.) Thoracoacromial artery & Lateral thoracic
- The thoracoacromial artery is distal or proximal to the 1st rib?
- The lateral thoracic artery is proximal or distal to the 1st rib?
- Where do these two branches come from?
1.) Thoracoacromial artery is proximal
2.) Lateral thoracic A is distal
3.) 2nd division of the Axillary artery
1.) The lateral border of pectoralis minor to the inferior border of teres major is what portion of the axillary artery?
2.) What branches come off this division of the axillary artery?
1.) 3rd division of axillary A
2. ) Subscapular , Post. Circumflex Humeral A., Ant. Circumflex Humeral A.
This artery arises inferior the subclavius and runs inferomedially to supply the subclavius muscle & muscles in the 1st and 2nd intercostal spaces
Superior thoracic A
The superior thoracic A. in the textbook arises from the 1st division of ________________________. In reality, it may come from somewhere else. What is another way to discern you are looking at the superior thoracic A.?
1.) Axillary artery
2.) See where it is supplying, should supply the 1st & 2nd intercostal spaces and the subclavius muscle
This artery branches off the second division of the axillary artery. It gives rise to 4 more branches (acromial, deltoid, pectoral and clavicular artery) and is deep to the clavicular head of the pectoralis major muscle
Thoracoacromial A.
What are the four branches coming off of the throacoacromial A.?
Clavicular
Acromial
Pectoral
Deltoid
This artery branches off the second division of the axillary artery and supplies pectoral, serratus anterior, intercostal muscles, axillary lymph nodes, and the lateral aspect of the breast
Lateral thoracic artery
This artery is the largest artery coming off the axillary artery. It descends along the lateral border of the subscapularis muscle of the posterior axillary wall, terminating by dividing into the circumflex scapular A and thoracodorsal A. In textbooks, this artery is in the 3rd division of the axillary artery
Subscapular Artery
1.) What branches off the subscapular Artery?
2.) Where does the the subscapular artery supply?
1.) Circumflex scapular artery & Thoracodorsal A
2.) Subscapular Artery
What muscle is supplied by Thoracodorsal Artery?
Latissimus artery
This artery is the smaller A of an anastomosing counterpart. It passes laterally and deep to the coracobrachialis muscle and biceps brachii.
Anterior circumflex humeral artery
What muscle is superficial to the anterior circumflex humeral artery?
1.) Coracobrachialis
2.) Biceps brachii
This artery is the larger of the pair anastomoses in the axillary region. It passes medially through the posterior wall of the axilla and supplies the deltoid, teres major/minor, and long head of triceps brachii
Posterior circumflex humeral artery
What is the largest artery branch coming off the axillary artery?
What branches off this artery?
Subscapular Artery
1.) Circumflex scapular artery
2.) Thoracodorsal artery supplying Latissmus dorsi
This artery is found deep to the rhomboids major and minor:
Dorsal scapular Artery
What are two anatomical markers for the Dorsal scapular Artery?
Inferior to Rhomboid M/m
Along the medial border of the scapula
1.) The suprascapular artery comes from:
2.) It forms an anastomoses with:
1.) Subclavian artery
2.) Dorsal scapular artery, circumflex scapular artery
Other than supplying the latissimuss dorsi, this artery can be found bordering the inferior angle of the scapula. This artery branched off:
Thoracodorsal Artery
Came from subscapular artery
Repetitive trauma like chronic crutch use or athletic activities involving repeated abduction or external rotation of the shoulder may lead to:
1.)
2.)
1.) Aneurysmal degeneration of the axillary artery
2.) Compress the trunks of the brachial plexus
What are the three kinds of fibers which constitute the Brachial plexus?
1.) Motor
2.) Sensory
3.) Sympathetic
Dorsal roots contain ______________ fibers.
Ventral roots contain ______________ fibers.
1.) Sensory fibers
2.) Motor fibers