1.  His, Lys, Arg

2.  Methyltransferases

1.  Active site residues

2.  Contact sites to other proteins

1.  Fibrous

2.  Globular

3.  Membrane-bound

1.  phi-betwen nitrogen and alpha carbon

2.  psi-alpha carbon and carbonyl carbon

Steps in protein folding (4)

1.  Nucleation

2.  Growth and coalesence (secondary)

3.  Readjustment for max stability

4.  Quaternary association

Enzymes

1.  Examples (2)

2.  Function

1.  Amylase, Glutamine synthetase

2.  Make unfavorable reaction favorable

Regulatory Proteins

1.  Example (1)

2.  Function

1.  Insulin

2.  Often hormones that control other processes in the body

Transport proteins

1.  Examples (4)

2.  Function

1.  Hemoglobin, HDL, LDL, Glucose transporter

2.  Transport through blood and lymph

Storage Proteins

1.  Examples (2)

2.  Function

1.  Ovalbumin, Casein

2.  Store other molecules or atoms for later use

Contractile and Motile Proteins

1.  Examples (3)

2.  Function

1.  Actin, Myosin, Tubulin

2.  Capable of causing movement of themselves or cells

Structural Proteins

1.  Example (1)

2.  Function

1.  Collagen

2.  Provide structural support to tissue (Fibrous)

Protective Proteins

1.  Examples (4)

2.  Function

1.  Immunoglobulin, Thrombin, Fibrinogen, Fibrin

2.  Cell defense against infectious agents and clot formation

Alzheimer's Disease

1.  Cause

Cancer

1.  Most common protein mutation

Creutzfeldt-Jacob Diease

1.  What is mutated

Cystic Fibrosis

1.  What is mutated

1.  What links peptidoglycan

2.  What does gram (+) have that gram (-) does not

1.  Lysine of one strand connected to alanine of other strand

2.  Pentaglycine linked peptidoglycans in Gram (+) while negative cross=links directly

1.  Simple lipids (2)

2.  Why are they simple?

1.  Terpenes and Steroids

2.  Do not contain fatty acids

Myristic Acid

1.  Long or short?

2.  Name of derivative with use?

1.  Short and easily encorporated into membrane

2.  Isopropyl myristate-used in cosmetics and topical medicinal preparations to achieve good absorption through the skin

Palmitic Acid

1.  Use

Stearic Acid

1.  Commonly combined with palmitic acid for what?

2.  Commonly found in

3.  Stearyl Alcohol used in

4.  Magnesium stearate used in

1.  Commercial use

2.  Cosmetics

3.  Lubricant, emulsifier, and thickener of ointments

4.  Used as a filling agent in medical pills and lubricant in pill production to keep pills from sticking to equipment during compression

1.  Alpha-linolenic (Omega 3)

2.  Linoleic (Omega 6)

Omega 3 made from Alpha-linolinic (2)

Eicosapentaenoic acid (EPA)

Docoseahexaenoic acid (DHA)

1.  Gamma-linolenic acid (GLA)

2.  Arachidonic acid (AA)

DHA

1.  Major FA in (3)

2.  Algae fish get it from

3.  Can body make and what from?

4.  Omega 3 or 6?

1.  Sperm; brain phospholipids; retina

2.  Schizochytrium

3.  Alpha linolenic acid and yes

4.  Omega 3

DHA

1.  Omega 3 or 6

2.  Highest concentrations in (1)

3.  What can it lower in blood (1)?

4.  What does lack of decrease (1)

1.  Omega 3

2.  Breast milk

3.  TAGs

4.  Decreased serotonin

Arachidonic Acid

1.  Made by

2.  Made from

3.  Inflammation downregulators made by AA (2)

1.  Mammals and not plants

2.  Linoleic acid (Omega 6)

3.  Lipoxin (Omega 6) and Resolvins (Omega 3)

Arthritis

Lupus

Asthma

Simple are same 3 fatty acids

Mixed have more than 1 type of fatty acids

What is the precursor for all phospholipids?

Phosphatidic acid

AKA MAKES GLYCEROPHOPHOLIPIDS WHICH YOU ATTACH A POLAR HEAD GROUP TO TO MAKE PHOSPHOLIPIDS

Lecithin

1.  Biochemical definition

2.  What is commercial compound a mixture of (3)

3.  Use (2)

4.  When derived from soy what is the benefit?

1.  Pure phosphatidylcholine

2.  Mixture of glycolipids, triglycerides, and phospholipids

3.  Emulsifier and lubricant

4.  Lower blood cholesterol and TAGs

Sphingolipids

1.  Sphingosine is what?

2.  What are fatty acids attached to in sphingolipids

3.  Components in ceramide (2)

4.  Components of spingomyelins (3)

1.  18C amino alcohol

2.  Spingosine backbone rather than glycerol

3.  Fattys acids and sphingosine

4.  Ceramide + phosphorous + another group (polar head group)-Imortant in nervous tissue

Terpenes

1.  What are they composed of

2.  How many units of #1 make a monoterpene

3.  Two important triterpenes

4.  Two important Tetraterpense

1.  Isoprene

2.  Monoterpene=2 isoprene

3.  Squalene and Lanosterol-cholesterol precursors

4.  B-carotene and lycopene-carotenoids

Long-chain FAs esterified to long-chain alcohols

Waxes are a source of lanolin

No, although plant sterols compete with cholesterol for intestinal absorption

Benecol-synthesized from plant sterols to use as butter substitue

1.  Cholesterol

2.  Hormones

3. Bile acids

Albumin

1.  Size

2.  Functions (4)

1.  66.4 kDa

2.  Stabilizes physical environment of blood; toxic waste removal; major transport vehicle; storage

Albumin Physical Environment Stabilization

1.  2 ways it does it

1.  Osmotic pressure

2.  Acid-base buffering (major macromolecular plasma anion)

Albumin Toxic Waste Removal

1.  Mechanism

1.  Fatty acids-can bind 11 at a time but usually just 1-4

2.  Bilirubin and heme

3.  Steroids-Only after steroid-specific binding protein (SSBP) is full, but more albumin than SSBP so usually has more total steroids bound

4.  Thyroxine

Albumin and drugs

1.  Binds what %

2.  Effects what as far as drugs are concerned

1.  90%

2.  Kinetics of drug binding

Alpha 1-antitrypsin

1.  Type of globulin

2.  What is it and what does it do?

3.  Protects (2)

4.  Deficiency causes

1.  Alpha globulin

2.  Is an alpha 1-antitrypsin (A1AT) that is a serine protease inhibitor (serpin) which degrades elastase from inflammatory cells

3.  Lungs and liver

4.  Inherited mutation leading to emphysema or liver disease...leading cause neonatal liver transplantation

Ceruloplasmin

1.  Type of globulin

2.  Metal ion necessary for function

3.  Function

1.  Alpha 2 globulin

2.  8 copper atoms

3.  Oxidizes free iron making it capable of binding to transferrin

Transferrin

1.  Type of globulin

2.  Function (3)

3.  How does it bind its atom?

1.  Beta globulin

2.  Iron transport, toxicity, immunity (keeps iron from bacteria)

3.  2 Fe in the 3+ state

Lipoproteins

1.  Function

2.  Structure

1.  Carry cholesterol, phospholipids, and TAGs in blood

2.  Core of lipids surrounded by cholesterol and phospholipid monolayer with embedded proteins

Defining feature of:

1.  HDL

2. LDL

3.  Chylomicrons

1.  33% protein 29% phospholipid

2.  50% cholesterol

3.  84% TAGs

High Cholesterol

1.  CVD risk assessment measured by what levels

2.  Does this always reflect diet?

1.  LDL

2. No

High TAGs

1.  Associated with

Fibrinogen

1.  What is it and what is it a precursor to?

2.  Basic clotting overview

3.  What breaks down clots

1.  Large blood plasma glycoprotein, fibrin

2.  Thrombin cross links and Factor XIII binds chains together

3.  Plasmin which is cleaved from plasminogen catalyzed by tissue plasminogen activator or streptokinase (must be given efore Factor XIII can stabilize the clot)

Hb

1.  Subunits

Mb

2.  Subunits

3.  What state must iron be in to bind oxygen

1.  2 Alpha and 2 Beta

2.  Single polypeptide chain

3.  Ferrous Fe2+, ferric is called methemoglobin (blue people)