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49 Cards in this Set
- Front
- Back
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Alanine |
Ala
A Nonpolar, Hydrophobic |
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Glycine
Structure? Abbreviations? Additional Information? |
Gly
G Polar, Uncharged |
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Valine
Structure? Abbreviation(s)? Additional Information? |
Val
V Nonpolar, Hydrophobic |
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Serine
Structure? Abbreviation(s)? Additional Information? |
Ser
S Polar, Uncharged |
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Leucine
Structure? Abbreviation(s) |
Leu
L Nonpolar, Hydrophobic |
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Cysteine
Structure? Abbreviation(s)? Additional Information? |
Cys
C Polar, Uncharged |
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Tyrosine
Structure? Abbreviation(s)? Additional Information? |
Tyr
Y Polar, Uncharged |
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Asparagine
Structure? Abbreviation(s)? Additional Information? |
Asn
N |
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Glutamine
Structure? Abbreviation(s)? Additional Information? |
Gln
Q Polar, Uncharged |
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Threonine
Structure? Abbreviation(s)? Additional Information? |
Thr
T Polar, Uncharged |
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Isoleucine
Structure? Abbreviation(s)? Additional Information? |
Ile
I Nonpolar, Hydrophobic |
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Phenylalanine
Structure? Abbreviation(s)? Additional Information? |
Phe
F Nonpolar, Hydrophobic |
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Tryptophan
Structure? Abbreviation(s)? Additional Information? |
Trp
W Nonpolar, Hydrophobic |
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Methionine
Structure? Abbreviation(s)? Additional Information? |
Met
M Nonpolar, Hydrophobic |
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Proline
Structure? Abbreviation(s)? Additional Information? |
Pro
P Nonpolar, Hydrophobic |
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Aspartic Acid
Structure? Abbreviation(s)? Additional Information? |
Asp
D Polar, Acidic |
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Glutamine Acid
Structure? Abbreviation(s)? Additional Information? |
Glu
E Polar, Acidic |
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Lysine
Structure? Abbreviation(s)? Additional Information? |
Lys
K Polar Basic |
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Arginine
Structure? Abbreviation(s)? Additional Information? |
Arg
R Polar, Basic |
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Histidine
Structure? Abbreviation(s)? Additional Information? |
His
H Polar, Basic |
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Proteins are made of ___.
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Amino Acids
Monomer Units |
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Amino acids have ___ isomers.
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L isomers only.
No D isomers. |
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Most amino acids have ___ configuration.
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S configuration
NOT R configuration |
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Proline is unique because ___ _____ _____.
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It is con
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These Amino Acids are positively charged at neutral pH.
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Lysine, Arginine
Histidine (can be) |
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These Amino Acids are acidic ___ and ____.
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Aspartic Acid
Glutamic Acid |
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What are other names of Aspartic Acid and Glutamic Acid?
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Aspartate
Glutamate |
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Primary Structure is ____.
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Amino acid sequence
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Secondary Structure of a protein is made up of _____, _____, _____, and _____.
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Alpha Helix
Beta pleated sheet Beta turn Omega Loop |
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Characteristics of Alpha Helix?
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Rodlike structure.
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Essentially all helices found in proteins are _____, which means they are _____wise.
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right-handed
clockwise |
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Beta plated sheets are made of _____ that are mostly _____ ______.
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made of two or more polypetide chains
that are mostly fully extended rather than tightly coiled. |
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Reversals are formed between _____ and _____.
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CO group and +3 NH group
By hydrogen bonding. |
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Motifs aka _____, have _____ functions and are combos of _____ structures.
One such is the __-__-__. |
Supersecondary Structure exhibit similar functions of 2nd structures (in many proteins). such as Helix-turn-Helix
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Primary Structure:
Secondary Structure: Tertiary Structure: Quaternary Structure: |
A.A. Sequence (1)
Spatial Arrangement within (2) Spatial Arrangement long r (3) Subunits interact (4) |
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How is Hemoglobin a Quaternary structure?
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Two subunits of
Alpha Beta |
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How are Disulfide Bonds Cleaved?
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beta-mercaptoethanol
breaks teh Cystines (S) |
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Which A.A. tend to be alpha helices?
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Alanine, Glutamate, Leucine
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Which A.A. tend to be beta strands?
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Valine, Isoleucine
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Which form Alpha Helix or Beta sheet is considered the default? and Why?
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Alpha Helix, due to beta being formed by steric clashes
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Acetyl groups are attached to the _____ terminal and provide _____.
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Amino terminal
providing resistance to degradation |
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What is an amide bond?
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Binding between Carboxyl group and amino group.
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Why is a peptide bond important?
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(1) resistant to hydrolysis
(2) Planar (3) H-bond donor= NH, acceptor CO (4) H bonding is distintive (5) peptide is uncharged, allows tightly packed globular structures (buried within protein interior) |
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Major elements of Secondary Structure?
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Alpha Helix
Beta Sheets |
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Alpha Helix is?
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Twisted polypeptide chains in a tightly packed rod.
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Beta Sheets?
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CO group bonded to NH group
More strands connected by NH -CO H bonds |
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Types of Sheets?
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Antiparallel, parallel, mixed
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Tertiary Structure
Water-soluble? |
Interior formed with Hydrophobic,
Exterior (surface area) of hydrophilic units. |
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Quaternary Structure made of?
and Bonded by? |
Subunits
Noncovalent Bonds |
