Term
Ionic bonds
Covalent bonds
Hydrogen bonds |
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Definition
I-weak
Covalent-strong
H-weakest between N or O |
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Term
Room temp and reg atm pressure liq water H bonds with #
Ice # causing |
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Definition
3.4
4 (max) regular crystal lattice |
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Term
| 4 biologically important H bonds: |
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Definition
1. Between the hydroxyl group of an alcohol and water
2. Between the carbonyl group of ketone and water
3. Between peptide groups in polypeptides
4. Between complementary bases of DNA (A-T, C-G) |
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Term
| Directionality of Hydrogen bond is greatest when the three atoms are |
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Definition
| straight line. Ideal geometry (less constrain for the molecule) results in weaker H bond. |
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Term
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Definition
| alpha amino group and alpha carboxylic group and one H atom bonded to the central C. Side chains are different |
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Term
| All nineteen chiral amino acids found in proteins are of |
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Definition
| L-configuration. (Glycine does not have a chiral carbon atom because two H atoms are attached to the carbon atom.) |
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Term
| Building blocks for protein= |
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Definition
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Term
| The amino acids with acid-dissociable side groups are |
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Definition
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Term
Peptide bond forms via
bond forms between:
Nucleophile: |
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Definition
| condensation rxn between hydroxyl group off carbonyl of one AA and the H off the amine. Bond is formed between carbonyl carbon and the nitrogen, water leaves. Amino groups are good Nucleophiles. |
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Term
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Definition
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Term
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Definition
free alpha amino group
free alpha carboxylic group |
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Term
| Numbering of polypeptides begins w/ |
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Definition
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Term
| What is the number of the C-terminal |
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Definition
| The number of AA in the polypeptide bc it is the last one |
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Term
Two molecules of Cysteine can:
Importance:
#insulin |
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Definition
| reversibly form a disulfide bond, covalent and very strong. Sulfur easily oxidizes. Disulfide bonds stabilize many proteins (insulin has 6 Cys) |
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Term
| Oxidizing (-SH) group to (-S-S) bond |
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Definition
| disulfide bond, covalent and very strong. Stablize proteins |
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Term
| Importance of The structure of the polypeptide hormone insulin in different mammals. |
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Definition
| Greater the structure difference the greater chance the host sees foreign protein which turns on immune response against it. |
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Term
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Definition
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Term
| A protein contains 512 amino acids (as determined from the gene that codes for the protein). What is its approximate MW? |
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Definition
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Term
| If a protein has a MW of 100,000, approximately how many amino acids are in that protein? |
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Definition
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Term
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Definition
| 3-D shape; folding of the polypeptide chain in 3-D space |
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Term
| Secondary structure, which is part of the conformation |
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Definition
| = the polypeptide's local conformation for its backbone. This incudes, but is not limited to, such structural motifs as alpha-helices and beta-sheets. |
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Term
| peptide bond characteristics- |
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Definition
tautomerization= double bond-like
6 atoms around the peptide bond form planar structure which constrains the #conformations that protein can form |
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Term
Peptide double bond character due to-
cannot- |
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Definition
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Term
| Alpha helix stabilized by -- between |
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Definition
Hydrogen bonds between alpha amino group and alpha carbonyl O on N, N+1
100, 104 and 123, 127 |
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Term
| Where are side chains in alpha helix |
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Definition
| Side chains stick out from helix and aren’t included in the structure. |
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Term
#AA per turn in alpha helix
pitch=
rise= |
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Definition
3.6 AA
5.4 Angstoms
1.5 Angstroms vertical |
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Term
% of AA in alpha helix is known via
Hb=
Chymotrypsinogen=
Keratin= |
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Definition
only determined experimentally
Hb 70
Chymo 0
Keratin 100 |
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