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
