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Acid base metbaolism symptoms-
Constipation, diuretics, vomiting |
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| Acid base metab. symptoms- Diarrhea, excess alcohol, diabetes, starvation |
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| Acid base metbab. symptoms- Brain stem injury, cystic fibrosis, bronchitis, narcotics |
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| Acid base metab. symptoms- Asthma, pneumonia, anxiety |
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Definition
unbranched polysac of alternating uronic acid and hexosamine residues
o Major component of ground substance (hyaluronic acid, chondroitin, keratan) |
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| What is a glycosidic bond and how are they denoted? |
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Definition
| Bond between the anomeric C of a monosaccharide and some other group/molecule. They are denoted typically 1-4 depending on whether the glycosidic bond is above or below the plane....alpha for below, beta for above plane. |
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Table sugar
Disaccharide formed from D-glucose and D-fructose
Glycosidic bond is between C1 of glucose and C2 of fructose
Is a nonreducing sugar because of its acetal linkage |
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Malt sugar
Two D-glucose monomers joined by an a (1→4)-glycosidic linkage
Produced by hydrolysis of starch by the enzyme diastase
Is a reducing sugar because the glucose moiety contains a hemiacetal functionality |
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| Reducing sugar or Non-reducing sugar? |
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Definition
| Reducing Sugars- Anomeric C's must be attached to O-H |
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Milk sugar
D-Galactose joined to a D-Glucose molecule by a b(1→4) glycosidic bond
Lactose is a reducing sugar because the glucose moiety contains a hemiacetal functionality |
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Results from partial hydrolysis of cellulose
Two D-glucose units joined by a b(1→4) glycosidic bond
It is a reducing sugar because the glucose moiety contains a hemiacetal functionality |
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| Name three critical glucans (made up only of glucose units) |
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| Three critical glucans are starch, glycogen, and cellulose |
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| What breaks glycogens anomeric linkages? |
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Definition
Glycogen Phosphorylase breaks a(1→4) linkages
Debranching Enzyme breaks a(1→6) linkages. Glycogen has a lot of branching and is "ready energy" for cell to use. It is stored in liver and muscle cells. |
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| How do you classify Delta and Omega fatty acids? |
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Definition
o Delta class = Position of double bond is counted from carboxyl group end of molecule
o Omega class = position of double bond is counted from non-carboxyl group (the methyl end) |
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Definition
| Only non-chiral amino acid |
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| 2 chiral carbons, hydrophobic |
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Definition
Basic, positively charged, hydrophilic.
Only amino acid that functions as a buffer in physiol. range. |
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Definition
Basic, positively charged, hydrophilic.
Only amino acid that functions as a buffer in physiol. range. |
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Term
| Stability and formation of the peptide bond |
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Definition
Hydrolysis of peptide bond favored energetically, but uncatalyzed reaction very slow.
Strong mineral acid, such as 6 M HCl, good catalyst for hydrolysis
Amino acids must be "activated" by ATP-driven reaction to be incorporated into proteins |
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| Secondary Protein structure |
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Definition
The three dimensional shape of a protein chain that results from hydrogen bonding between peptide bonds on the polypeptide chain
Large scale patterned H-bonding involving the backbone components of the polypeptide chain
-Helix (a-keratin)
-Pleated Sheet (silk) |
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| Primary protein structure |
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Definition
| The sequence of amino acids in a peptide or polypeptide starting at the N-terminal end and going to the C-terminal end. |
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| Alpha-helix destabilized by what two amino acids? |
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| critical for collagen stability, requires vitamin c |
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| Tertiary protein structure |
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Definition
Overall 3-D shape of a protein, highest order for a single polypeptide. Two basic types are globular and fibrous. Five classes of tertiary interactions/bonds
Hydrophobic force (attraction)
Van der Waals interactions
Side chain H-bonding
Salt linkages
Disulfide linkages
All involve interactions between side chains of amino acids in chain
Disulfide linkages are covalent bonds; others are weak attractions |
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| Quaternary protein structure |
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Definition
o Bonds: electrostatic (charged) interactions, H bonds, hydrophobic interactions
o Requires participation from other mole = organic (enzymes), inorganic (metal ions) |
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Definition
Proteinaceous infectious particles. Smaller than smallest known virus
Not yet completely characterized
Most widely accepted theory
Prion = Proteinaceous infectious particle with no DNA or RNA detected.
Normal Protein
PrPC (C for cellular) comprised of 254 residues
Glycoprotein normally found at cell surface inserted in plasma membrane with a GPI anchor. Found on most cell types, but most abundant in the CNS |
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| Normal protein characteristics |
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Definition
Secondary structure dominated by alpha helices
Easily soluble
Easily digested by proteases
Encoded by PRNP gene (in humans)
Located on human chromosome 20 |
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| Abnormal Protein characteristics |
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Definition
Secondary structure dominated by alpha helices
Easily soluble
Easily digested by proteases
Encoded by PRNP gene (in humans)
Located on human chromosome 20. Insoluble in all but strongest solvents
Highly resistant to digestion by proteases
Survives in tissues post-mortem
Extremely resistant
Heat, normal sterilization processes, sunlight
No detectable immune response |
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| Creutzfeld- Jacob Disease (CJD) caused by/how? |
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Definition
If protein folding goes wrong...in general misfolded proteins get degraded immediately
In some cases, they can form aggregates, which might be difficult to get rid of. Aggregates can cause CJD. |
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Definition
• R is neutral, pI = 6
• R contains carboxyl group, pI = 3
• R contains amino group, pI = 10 |
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| How are O and N glycosidic bonds created? |
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Definition
o O-glycosidic bonds = hydroxyl groups of ser + thr
o N-glycosidic bonds = side chain amide nitrogen of asp |
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