Busy. Please wait.
or

show password
Forgot Password?

Don't have an account?  Sign up 
or

Username is available taken
show password

why


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
We do not share your email address with others. It is only used to allow you to reset your password. For details read our Privacy Policy and Terms of Service.


Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
Don't know
Know
remaining cards
Save
0:01
To flip the current card, click it or press the Spacebar key.  To move the current card to one of the three colored boxes, click on the box.  You may also press the UP ARROW key to move the card to the "Know" box, the DOWN ARROW key to move the card to the "Don't know" box, or the RIGHT ARROW key to move the card to the Remaining box.  You may also click on the card displayed in any of the three boxes to bring that card back to the center.

Pass complete!

"Know" box contains:
Time elapsed:
Retries:
restart all cards
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

BioChem quiz 1

Amino acids and HW 1

QuestionAnswer
Four groups of biomolecules 1. Protein 2. Carbohydrates 3. Nucleic Acids 4. Lipids
zwitter ions ions that have both a positive and negative charge-- ex. all amino acids
Chiral carbon carbon with 4 different substituents bound to it
enantiomers a stereoisomer that is a mirror image of the other structure
2 laws of thermodynamics 1. you can't create or destroy energy 2. entropy tends to increase
4 non-covalent (weak) interactions in aqueous solution 1.Ionic bonds 2. hydrogen bonds 3. Hydrophobic interactions 4 Van Dar Waals forces
5 groups of the 20 amino acids 1. non polar, aliphatic 2. polar, uncharged 3. aromatic 4.Positively charged 5. Negatively charged
Nonpolar, aliphatic R groups (biggest group) (7) 1) glycine 2) alanine 3) proline 4)Valine 5)leucine 6) Isoleucine 7)methionine
Nonpolar, aliphatic R group characteristics 1) mostly hydrophobic in nature 2) like hydrophobic interactions most of the 4 interactions
Polar, uncharged R groups (aa) (5) 1) serine 2) Threonine 3) Cysteine 4) Asparagine 5) Glutamine
2 amino acids that have sulfur in them 1) cysteine 2) Methionine
Aromatic R groups (aa) (3) 1) phenylalanine (non polar) 2) Tyrosine (polar) 3) Tryptophan (non polar)
Positively charged R groups (aa) (3) 1) lysine 2) arginine 3) Histidine
Negatively charged R groups (aa) (2) 1) aspartate (aspartic acid) 2) Glutamate (glutamic acid)
4 processes to change a.a. structure 1) methylation 2) Phosphorylation 3) Carboxylation 4) Hydroxylation
Selenocysteine -sometimes called the 21st a.a.
Citrulline and Ornithine metabolites that are intermediates in the urea cycle
Carnitine metabolite that transports fatty acids to the mitochondria
Creatine metabolite that is an intermediate energy storage compound in skeletal muscle
Isomer any two molecules with the same molecular formula but a different arrangement of molecular groups
Conformation A spatial arrangement of substituent groups that are free to assume different positions in space, without breaking any bond, because of freedom of rotation
Stereoisomer Compounds that have the same composition and the same order of atomic connections but different molecular arrangements
Configuration The spatial arrangement of an organic molecule that is conferred by the presence of either (1) double bonds, about which there is no freedom of rotation, or (2) chiral centers, around which substituent groups are arranged in a specific sequence.
Diastereomers stereoisomers that are not mirror images of one another
Glycine Characteristic only aa that is not chiral
Proline characteristic R and alpha aimno group form a ring---impacts conformation of protien.
Polar uncharged R group characteristics important for hydrogen bonding
Aromatic R group characteristics large, bulky aa that have aromatic rings---absorption maximum at 280nm---important for Protien biochemistry
Tyrosine and Tryptophan characteristic both absorb ultra-violet light
Positively charged R group characteristics Basic aa that can form Ionic bonds
Lysine and Arginine characteristic pKr > 7.0
Histidine characteristic pKr close to 7.0--- plays a major role in enzyme function
Negatively charged R group characteristics Acidic (pKr low) aa that form ionic bonds--- "-ate": deprotonated organic acid
4 abbreviations that are not the first 3 letter of the aa 1) Isoleucine (Ile) 2) Tryptophan (trp) 3) Asparagine (Asn) 4) Glutamine (Gln)
How do you find neutral aa pI? pK1 + pK2 / 2
How do you find Acidic aa pI? pK1 + pKr / 2
How do you find Basic aa pI? pKr + pK2 / 2
condensation putting together --- catalyzed by ribosomes --- produces water
Hydrolysis pulling apart --- catalyzed by proteases/ peptidases
Amide bond formed through condensation of carboxyl and amino groups --- called peptide bone on amino acid polymers
Peptide bond condensation between the alpha carboxyl group and alpha amino group
oligopeptide polymers of a few amino acids (building blocks)
Polypeptide Mw? Mw < 10,000 g/mol
Protien Mw? Mw > 10,000 g/mol
#1 amino acid in polypeptide? amino acid that is next to the N-terminus
Tripeptide mad up of? 3 amino acids and 2 peptide bonds
Created by: Enorum1109