Term
| Hydrophobic ("fear water") interactions are |
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Definition
| weak van der Waals forces between groups that have low solubility in water and thus higher solubility in non-polar solvents. |
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Term
| Phobic molecules group together because |
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Definition
| high volume=lower surface area=less intrxn |
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Term
| major driving force of 3d globular protein- |
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Definition
| hydrophobicity- phobic molecules buried interioly |
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Term
| water dissolves crystalline salts by |
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Definition
| partially neutralizing the ions, electrostatic attractions necessary for lattice formation are weakened |
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Term
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Definition
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Term
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Definition
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Term
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Definition
| charge separation via resonance |
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Term
| polypeptide in lipid layer of membrane |
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Definition
| alpha helix about 20AA length |
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Term
Clustering lipids increases-
which decreases order of- |
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Definition
entropy
order of water. Water likes water |
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Term
| Alpha helix common in -- bc |
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Definition
| hydrophobic envir. bc more bonds formed=more stable cmpd and alpha helix increases H bonds |
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Term
| transmembrane AA are likely |
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Definition
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Term
| Beta=adrenergic receptor bindsex of- |
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Definition
alpha helical structure of transmembrane segments of proteins 7X
epinephrine |
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Term
Beta sheet hydrogen bonds
compared with Helix |
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Definition
| distant from one another in primary seq where as in helix the AA H bond are close (123 and 127) |
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Term
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Definition
| two polypeptide segments run in opposite directions (i.e., N to C and C to N) |
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Term
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Definition
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Term
| Which B sheet more stable why |
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Definition
| anti parallel more stable bc H bonds are close to linear in the former and more bent in the latter. Anti-parallel beta sheets occur in proteins more commonly than do parallel beta sheets. Often more than two polypeptide segments are involved in making beta-sheet segments of proteins. |
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Term
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Definition
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Term
| proteins in aq envrn assume |
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Definition
| globular 3D shape due to hydrophobic intrxns |
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Term
| proteins that have fibrous shape have a lot |
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Definition
| alpha helices and beta sheets |
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Term
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Definition
| loss of conformation. Does not alter primary structure. No peptide bonds broken. |
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Term
| Denatured proteins are -- soluble in water |
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Definition
| less bc phobic AA are now exposed to aq solvent instead of being buried |
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Term
| Denaturing agents disrupt |
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Definition
| weak bonds that stabilize 2nd and 3rd structure (H bonds) |
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Term
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Definition
| The increased thermal motion of atoms breaks the weak non-covalent bonds.Cooking is a great example of this type of denaturation. It not only sterilizes food but also precipitates many of the once-soluble proteins. |
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Term
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Definition
| alcohol less polar than water makes hydrophobic groups more soluble in alcohol. they are buried, but to interact with alcohol they become less buried via unfolding. |
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Term
| 70% Alcohol instead of 95% to sterilize skin: |
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Definition
| the latter precipitates proteins so fast that a solid outer barrier can form in some microorganisms, resulting in protection of the genetic apparatus. Thus some microorganisms survive and can multiply. Seventy percent alcohol acts more slowly and thus can penetrate into the core of most microorganisms, resulting in protein denaturation throughout the cell. Nowadays isopropyl alcohol is used more often than ethanol. |
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Term
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Definition
scale of seconds'
aided by chaperones |
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Term
| misfolding protein diseases |
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Definition
| cystic fibrosis, alzheimers, mad cow |
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Term
| proteins comprised of more than one polypeptides termed "subunits"= |
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Definition
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