Busy. Please wait.

show password
Forgot Password?

Don't have an account?  Sign up 

Username is available taken
show password


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.

By signing up, I agree to StudyStack's Terms of Service and Privacy Policy.

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.

Remove ads
Don't know
remaining cards
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:
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

AA & Protein Struct

Medical Biochemistry

Nonpolar, aliphatic amino acids (7) -Hydrophobic and GENERALLY found in interior of water soluble proteins -Gly, Ala,Val, Leu, Ile, Pro, Met
Aromatic amino acids (3) -Hydrophobic and often found in interior of water soluble proteins -Phe, Tyr, Trp
Polar, uncharged amino acids (5) -Found in both the interior and exterior of protein structure -Ser, Thr, Cys, Asn, Gln
Amino acids with ionizable side chains (5) -R group can donate or accept protons -Asp, Glu, Lys, Arg, His
Two special/ unique amino acids, why? Gly- only amino acid not having an asymmetric/ chiral alpha center Pro- secondary alpha amine generated by the R group,forming a ring
Sulfure containing amino acids Met and Cys
Amino acids with carboxylic side chains (2) and amino-like side chains (3) -negatively charged/ acidic at pH of 7 -Asp and Glu -Positively charged and basic -Lys, Arg, and His
Structure and deffinition of Peptide Bonds -connect amino acids to form polypeptide chains -dehydration between a-carboxyl of one amino acid and a-amino group of another -hybrid of 2 resonance states, imparting partial double bond characteristics preventing free rotation around bond -planar & f
Primary Structure -Amino Acid sequence -determines 3D structure and biological function of protein -Amino (N) terminus or free amino goup at one end -Carboxyl (C) terminus or free carboxyl group at one end
Written form of a polypeptide chain N-terminus to C-terminus
Secondary Structure -segment of polypeptide chain that has regular repeating structure -result from H-bonding interactions between C=O and H-N groups -a-helices and B-pleated sheets
a-helices vs. B-pleated sheats a-helices-rod shaped,tight spirals (r-handed) -each C=O h-bonds to H-N 4 amino acids down chain B-pleated sheets-2+ polypeptide chains align side by side -interchain H-bonding of C=O and N-H groups -R groups project up and down -Paralell or Antiparal
Sharp bend in primary structure -Pro residue disrupts H-bonding forming bend and further disrupting H-bonding down stream
Reverse turns in B-pleated sheets -typically forms at water-peptide interface of protein surface -H-bonding between C=O of 1st and H-N of 4th amino acid stabalize -salt bridges,metal ions,disulfide bonds add more stability -often in antiparalell sheets
Supersecondary Structures aka Structural Motifs -assist in protein folding -interactions between newly folded and previously formed structures
Tertiary Structures give 1 example... -3D structure -interaction of secondary structures and non-ordered regions of polypeptide chain -Myoglobin (Mb)
Prosthetic groups What is a protein that lacks the prosthetic group. -organic molecules permanently bound to protein -Apoproteins lack the prosthetic group
Final functioning protein structure... How are they stabalized? -Native structure -folded through favored pathways in cooperative manner -supersecondary structures, H-Bonding, salt bridges, hydrophobic forces and van der Waal's attractions -folding assisted by chaperones
What can cause proteins to become disrupted or denatured? Why? -increase in temperature -detergents -pH extremes -agents like urea and guanidinium hydrochloride -these factors disrupt non-covalent bonds that maintain the folded conformation
Quaternary Structure give an examples... -Proteins that contain 2+ subunits -Hemoglobin (Hb
Oxygen binding to a heme... -binds 4 O -doesn't bind with equal affinity -as O increases, heme binds O more efficiently -binding O to a-Hb transforms Hb from T form to R form (valine residue moved from B-Hb binding sights) -causes positive allosterism
Allosterism -binding of one molecule influences the ability of other molecules to bind at different sights -positive and negative -binding of O to Hb
2,3-BPG, CO2, and H influential behavior in Hb 2,3-BPG- stabilizes T form by binding in central cavity H- binds to histidine,+ charge residues form salt bridges w/ aspartate, stabilize T form CO2- facilitates deprotonization in lungs and R form, binds to N terminal forms carbamates and T form
HbF v. HbA1 Why do the differences matter? -HbF= predominant form in fetus (2nd and 3rd trimester) =increases O affinity by reducing affinity for 2,3BPG = Histidine replaced with serine -HbA1=tetramer of a2B2, most common in adults (90%)
Hemoglobinopathy - mutant hemoglobins giving rise to clinical problems - unstable structure increases or decreases O affinity or increases rate of oxidation of heme Fe2+ to Fe3+
Post translational modification -modifications that occur after protein has been synthesized -occur while growing polypeptide is still attached to ribosome
Protein Domains -lobes, caused by folding of large polypeptide chains -segregate structure and/or function -domains connected by flexible linker regions -different enzyme activities sequestered in distinct, folded domains
Collagen and the importance of amino acid comp and sequence, unusual amino acids and their function, importance of vitamin-C and iron in formation -most abundant protein (1/4 ttl proteins) -35% glycine + 11% alanine, w/ proline -4-hydroxyproline(V-C) + 5-hydroxylysine allow triple helix -glycine every 3rd sequence=structure and stability -peptide-proline,peptide-hydroxyproline=strength and rigid
Proteins in: Sickle Cell Anemia, Scurvy, and Prion disease Sickle Cell Anemia=valine instead of glutamate (sticky hydrophobic patch B subunits) Scurvy=insufficient Vit. C, crucial forming hydroxyproline and insufficient hydroxylysine (extracellular covalent cross links and glycosylation. Prion=misfolded protein
Created by: MastamikeOD

Browse or Search millions of existing flashcards     Create Flashcards plus a dozen other activities