1/6/20, 9:16:32 PM
Compare Results
New File:
Old File:
First Aid for the USMLE Step 1 2020, Thirtieth
FA 2019.pdf
versus edition-1.pdf
24 pages (293.11 MB)
26 pages (109.99 MB)
1/5/20, 12:57:57 PM
1/5/20, 12:52:18 PM
BY u/verified-idiot
To the only girl i've ever loved, to soufia.
BLUE new in FA 2020
YELLOW text of FA 2019 was edited; the note box next to the yellow highlight will show the difference between
them the old text and the new text of FA 2020
Some pages might look scary! because of note boxes and highlighting , but it is not, my recommendation for
you is to study your book and after than look for the new stuff and edits.. I DONT recommend comparing while
you are studying since it will consume your time.
Go to First Change (page 1)
file://NoURLProvided[1/6/20, 9:16:32 PM]
,HIGH-YIELD PRINCIPLES IN
Pharmacology
“One pill makes you larger, and one pill makes you small.” ` Pharmacokinetics and
—Grace Slick Pharmacodynamics 230
“I was under medication when I made the decision not to burn the tapes.” ` Autonomic Drugs 236
—Richard Nixon
` Toxicities and
“I wondher why ye can always read a doctor’s bill an’ ye niver can read his Side Effects 248
purscription.”
—Finley Peter Dunne ` Miscellaneous 253
“One of the first duties of the physician is to educate the masses not to
take medicine.”
—William Osler
Preparation for pharmacology questions is straightforward. Know all the
mechanisms, clinical use, and important adverse effects of key drugs and
their major variants. Obscure derivatives are low-yield. Learn their classic
and distinguishing toxicities as well as major drug-drug interactions.
Reviewing associated biochemistry, physiology, and microbiology
concepts can be useful while studying pharmacology. The exam has a
strong emphasis on ANS, CNS, antimicrobial, and cardiovascular agents
as well as on NSAIDs, which are covered throughout the text. Specific
drug dosages or trade names are generally not testable. The exam may
use graphs to test various pharmacology content, so make sure you are
comfortable interpreting them.
229
, 230 SEC TION II PHARMACOLOGY `P̀HARMACOLOGY—PHARMACOKINETICS AND PHARMACODYNAMICS
``
PHARMACOLOGY—PHARMACOKINETICS AND PHARMACODYNAMICS
Enzyme kinetics
Michaelis-Menten Km is inversely related to the affinity of the [S] = concentration of substrate; V = velocity.
kinetics enzyme for its substrate. Saturation
Vmax is directly proportional to the enzyme
Velocity (V)
Vmax
concentration. Km = [S] at 1⁄2 Vmax
1⁄2 Vmax
Most enzymatic reactions follow a hyperbolic
curve (ie, Michaelis-Menten kinetics); Km [S]
however, enzymatic reactions that exhibit a
sigmoid curve usually indicate cooperative Effects of enzyme inhibition
Saturation
kinetics (eg, hemoglobin).
Velocity (V)
Vmax
Competitive inhibitor (reversible)
1⁄2 Vmax
Noncompetitive inhibitor
Km [S]
Lineweaver-Burk plot The closer to 0 on the Y-axis, the higher the 1
Uninhibited
Km
Vmax. V slope =
1 Vmax
The closer to 0 on the X-axis, the higher the Km. 1
− Km Vmax
The higher the Km, the lower the affinity.
1
Competitive inhibitors cross each other, [S]
whereas noncompetitive inhibitors do not. Effects of enzyme inhibition
Noncompetitive inhibitor
Kompetitive inhibitors increase K m. Competitive inhibitor (reversible)
1
V Uninhibited
1
− Km 1
Vmax
1
[S]
Competitive Competitive
inhibitors, inhibitors, Noncompetitive
reversible irreversible inhibitors
Resemble substrate Yes Yes No
Overcome by [S] Yes No No
Bind active site Yes Yes No
Effect on Vmax Unchanged
Effect on Km Unchanged Unchanged
Pharmacodynamics potency efficacy efficacy
Compare Results
New File:
Old File:
First Aid for the USMLE Step 1 2020, Thirtieth
FA 2019.pdf
versus edition-1.pdf
24 pages (293.11 MB)
26 pages (109.99 MB)
1/5/20, 12:57:57 PM
1/5/20, 12:52:18 PM
BY u/verified-idiot
To the only girl i've ever loved, to soufia.
BLUE new in FA 2020
YELLOW text of FA 2019 was edited; the note box next to the yellow highlight will show the difference between
them the old text and the new text of FA 2020
Some pages might look scary! because of note boxes and highlighting , but it is not, my recommendation for
you is to study your book and after than look for the new stuff and edits.. I DONT recommend comparing while
you are studying since it will consume your time.
Go to First Change (page 1)
file://NoURLProvided[1/6/20, 9:16:32 PM]
,HIGH-YIELD PRINCIPLES IN
Pharmacology
“One pill makes you larger, and one pill makes you small.” ` Pharmacokinetics and
—Grace Slick Pharmacodynamics 230
“I was under medication when I made the decision not to burn the tapes.” ` Autonomic Drugs 236
—Richard Nixon
` Toxicities and
“I wondher why ye can always read a doctor’s bill an’ ye niver can read his Side Effects 248
purscription.”
—Finley Peter Dunne ` Miscellaneous 253
“One of the first duties of the physician is to educate the masses not to
take medicine.”
—William Osler
Preparation for pharmacology questions is straightforward. Know all the
mechanisms, clinical use, and important adverse effects of key drugs and
their major variants. Obscure derivatives are low-yield. Learn their classic
and distinguishing toxicities as well as major drug-drug interactions.
Reviewing associated biochemistry, physiology, and microbiology
concepts can be useful while studying pharmacology. The exam has a
strong emphasis on ANS, CNS, antimicrobial, and cardiovascular agents
as well as on NSAIDs, which are covered throughout the text. Specific
drug dosages or trade names are generally not testable. The exam may
use graphs to test various pharmacology content, so make sure you are
comfortable interpreting them.
229
, 230 SEC TION II PHARMACOLOGY `P̀HARMACOLOGY—PHARMACOKINETICS AND PHARMACODYNAMICS
``
PHARMACOLOGY—PHARMACOKINETICS AND PHARMACODYNAMICS
Enzyme kinetics
Michaelis-Menten Km is inversely related to the affinity of the [S] = concentration of substrate; V = velocity.
kinetics enzyme for its substrate. Saturation
Vmax is directly proportional to the enzyme
Velocity (V)
Vmax
concentration. Km = [S] at 1⁄2 Vmax
1⁄2 Vmax
Most enzymatic reactions follow a hyperbolic
curve (ie, Michaelis-Menten kinetics); Km [S]
however, enzymatic reactions that exhibit a
sigmoid curve usually indicate cooperative Effects of enzyme inhibition
Saturation
kinetics (eg, hemoglobin).
Velocity (V)
Vmax
Competitive inhibitor (reversible)
1⁄2 Vmax
Noncompetitive inhibitor
Km [S]
Lineweaver-Burk plot The closer to 0 on the Y-axis, the higher the 1
Uninhibited
Km
Vmax. V slope =
1 Vmax
The closer to 0 on the X-axis, the higher the Km. 1
− Km Vmax
The higher the Km, the lower the affinity.
1
Competitive inhibitors cross each other, [S]
whereas noncompetitive inhibitors do not. Effects of enzyme inhibition
Noncompetitive inhibitor
Kompetitive inhibitors increase K m. Competitive inhibitor (reversible)
1
V Uninhibited
1
− Km 1
Vmax
1
[S]
Competitive Competitive
inhibitors, inhibitors, Noncompetitive
reversible irreversible inhibitors
Resemble substrate Yes Yes No
Overcome by [S] Yes No No
Bind active site Yes Yes No
Effect on Vmax Unchanged
Effect on Km Unchanged Unchanged
Pharmacodynamics potency efficacy efficacy
