• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/11

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

11 Cards in this Set

  • Front
  • Back

Positive Amino Acids

Arginine, Arg, R


Lysine, Lys, K


Histidine, His, H

Negative Amino Acids

Aspartic Acid, Asp, D


Glutamic Acid, Glu, E

Uncharged Polar

Asparagine, Asn, N


Glutamine, Gln, Q


Serine, Ser, S


Threonine, Thr, T


Tyrosine, Tyr, Y

Nonpolar

Alanine, Ala, A


Glycine, Gly, G


Valine, Val, V


Leucine, Leu, L


Isoleucine, Ile, I


Proline, Pro, P


Phenylalanine, Phe, F


Methionine, M


Tryptophan, W


Cysteine, C

Protein to Protein binding Methods

Surface- String


Helix-Helix


Surface-Surface

BARSTAR! stops who?

Barnase

Common PTMs (covalent)

-phosphate on Ser,Thr, or Tyr


-methyl on Lys


-acetyl on lys


-Palmityl group on Cys


-N-acetyglucosamine on Ser or Thr

Phosphorylation is an example of?

A covalent post translational modification.

Retinal

is a type of Vitamin A that binds to opsin proteins



Ubiquitination and types

The addition of ubiquitin


C terminus bound to Lys residue of substrate


Mono-Ub: endocytosis, protein transport, DNA repair, and histone regulation


Multi-Ub: endocytosis


Poly-Ub K63: endocytosis, DNA repair, and signaling


Ploy-Ub K48: proteasomal degradation



examples of multiple modification regulations

Src Kinase:Removes phosphate->activates ligand that binds to SH3 domain-> kinase phosphorylates tyrosine to self activate.




P53: causes DNA damage, hypoxia, heat/cold shock, mitotic spindle damage.-> leads to Cell cycle arrest, DNA repair, Apoptosis, Senescence