Proteins/Amino Acids

Hemoglobin contains ____ hemes and can potentially associated with ____ oxygen molecules.

4 4

Humans can only synthesize ____ of the 20 common amino acids. Other must be consumed in diet. PVT TIM HALL

9

Non-essential Amino Acids : Mnemonic [ Almost All Girls Go Crazy After Getting Taken Prom Shopping ]

Alanine Asparagine Glutamate Glutamine Cysteine Aspartate Glycine Tyrosine Proline and Serine

Pyruvate gives rise to: 1. 2. 3. 4.

Alanine Valine Leucine Isoleucine

The absence of Tyrosine from a genetic defect can cause:

Albinism

What provides 80% of colloid osmotic pressure of the plasma? This protein is one of the most hydrophilic plasma proteins.

Albumin

What two AA's have free amino groups on their R group that attracts H+, giving them a positive charge which makes them perfect for bonding to neg. charged phosphate groups?

Arg. and Lys.

Oxaloacetate gives rise to aspartate which in turn is the precursor of: 1. 2. 3. 4.

Asparagine methionine threonine lysine

Amino Acids are degraded to:

Carbon Dioxide Water Urea

_____ residues react to form a disulfide bond.

Cysteine

Sulfur Amino Acids

Cysteine Methionine

Collagen and Elastin are similar in that they both contain covalent crosslinks derived from allysine. Crosslinks of Elastin contain _____ which is not present in Collagen.

Desmosine

This bond helps stabilize the structure of protein. It is formed when two sulfhydryl (-SH) groups of Cysteines. This bond is called

Disulfide Bond

Drop in Albumin can lead to what:

Edema

alpha-ketogluturate gives rise to glutamate, which in turn is a precursor of: 1 2 3

Glutamate Proline Argine

Acidic Amino Acids

Glutamate Aspartate

Type I collagen aa sequence has a _____ every third position

Glycine

What is the only non-chiral amino acid?

Glycine

Elastin has an abhorrent amino acid composition, with higher proportions of what 3 AA?

Glycine Alanine Proline

3-phosphoglycerate gives rise to serine, which in turn is the precursor of: 1 2

Glycine Cysteine

Type I collagen - Most abundant in the body. Has 33% - 10% - It also contains Hydroxyproline and Hydorxylysine

Glycine Proline

What amino acids can be formed from Serine? Select all that apply Methionine glycine proline arginine cysteine

Glycine Cysteine

Small Amino Acids

Glycine and Alanine

Cytochromes are in general, membrane bound ________ that contain heme groups and carry out ___ ____.

Hemoproteins Electron Transport

Ribose-5-phosphate gives rise to:

Histidine

Which AA carry a positive charge on the side chain, making them basic?

Histidine Arginine Lysine

Basci Amino Groups (HAL)

Histidine Arginine Lysine

What is attached to an alpha carbon?

Hydrogen Atom Carboxyl Group (COOH) Amino Group (NH2) 4th group that differs with each amino acid

Patients with Vitamin C deficiency form a collagen with insufficient: Isoleucine Hydorylysine Valine Hydroxyproline

Hydroxyproline

Tertiary structure

Irregular folding of polypeptide chain Three dimensional confirmation

All amino acids found in proteins are of what configuration?

L-Configuration

Most plasma proteins are derived from the:

Liver

Elastin crosslinks involve:

Lysine Oxidized lysine residues (Allysine) Desmosine

Purely Ketogenic amino acids:

Lysine Leucine

Histones contain large portions of what two AA's?

Lysine and Arginine

The amorphous elastin is surrounded by MICROFIBRILS. The most important ficrofibrillin-1 is defective in:

Marfan's Syndrome

Three major purposes of Amino Acids 1. M 2. P 3. S

Metabolic energy Protein Synthesis Synthesis of many products including: Heme, Purines, Pyrimidines, coenzymes, melanin, and biogenic amines

Carbon Monoxide binds similarly to heme iron atoms as oxygen, but the binding of Carbon Monoxide is _____ _____ that that of oxygen. This can lead to asphyxiation and carbon monoxide poisoning

Much stronger

In humans, tyrosine is synthesized from:

Phenylalanine

Aromatic Amino Acids

Phenylalanine Tyrosine Tryptophan

Essential Amino Acids PVT TIM HaLL

Phenylalanine Valine Threonine Tryptophan Isoleucine Methionine Histidine Leucine Lysine

Which AA restricts the range of rotation of the alpha carbon in the peptide bond?

Proline

Quaternary Structure

Refers to spatial arrangement of subunits in a protein that consists of more than one polypeptide chain Examples: Hemoglobin and antibody molecules

Primary Structure -

Sequence of AA held together by peptide bonds

Hydroxyl Amino Acids

Serine Thyronine

Phosphoenolpyruvate and erythrose-4-phosphate produces _____, which is converted to Chorismate. ______ then gives rise to tryptophan, tyrosine, and phenylalanine. (this only occurs in plants and bacteria, not humans)

Shikimate Chorimate

Secondary Structure

Spatial arrangement of a portion of a polypeptide chain determined by the AA's present. Alpha Helix (Coiled) B-Pleated Sheets (ZigZag) B-Hairpin turns (Reverse turns)

Basic structural component of collagen fibrils:

Tropocollagen

Polypeptide subunit of elastin fibrils:

Tropoelastin

Serotine, Melatonin, niacin and nicotinamide are formed from the essential AA.

Tryptophan

Dopamine, thyroid hormones, melanin, norepinephrine, and epinephrine are synthesized from what Amino Acid?

Tyrosine

Phenylalanine catalyzed the transformation of phenylalanine to:

Tyrosine

Branched-Chain Amino Acids (have hydrophobic side chains)

Valine Leucine Isoleucine

What vitamin is req. for the hydroxylation of proline? Hydroxyproline is a constituent of collagen that provides stability to the triple-helicle structure of collagen via hydrogen bonding

Vitamin C

Best method to determine three dimensional structure of a protein?

X-ray difraction