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PKa's and Amino Acids

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achapss's version from 2017-10-03 22:07

Section

Question Answer
GlycineGly, G
AlanineAla, A
ValineVal V
LeucineLeu L
IsoleucineIle I
MethionineMet M
ProlinePro P
PhenylalaninePhe F
TryptophanTrp W
LysineLys K
ArginineArg R
HistidineHis H
SerineSer S
ThreonineThr T
TyrosineTyr Y
CysteineCys C
AsparagineAsn N
GlutamineGln Q
GlutamateGlu E
AspartateAsp D
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Section

Question Answer
Pk C terminus3.5
Pk Cys8.4
Pk Asp3.9
Pk Glu4.1
Pk His6.0
Pk N terminus9.0
Pk Tyr10.5
Pk Lys10.5
Pk Arg12.5
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section

Question Answer
Thermal Motionsoccurring at internal physiological pH
Brownian Motionrandom movements allowed by thermal energy in a solution that initiates other interactions
Hydrophobic Effectorganization of solvent insoluble in water, molecules are more cohesive with each other than water and are only attracted to each other due to increase in energy when H2o is released, powers protein folding
Entropylack of order, energy existing
Enthalpytotal heat, energy being lost
Bulk Solventthe highly entropic part of solvent
Dielectric Constanttells us how permissive to movement of electrical charge something is, D, can be controlled by enzymes
Conjugated bondlower quality and less chance of accepting a proton
What is Kw?water constant 1.0X10^-14 M^2
Conjugate Acidforms when a base binds a proton
Aciduniversal donor
Baseuniversal acceptor
Covalent Bondsshare do not donate
Ionic Bondscomplete transfer of e- loses and then becomes an ion
Intramolecularhold atoms together within a molecule (Covalent and ionic)
Intermolecularexist between molecules (Hbond dipoles, LDF)
H bondbetween H and NOF, a H connected to a C atom can not participate
Dipole Dipolepartial charges of molecules interacting
London Dispersion Forces or Van Der Waalsalways going on, weakest interactions, more between atoms with more electrons
Zwitterionshave both positive and negative charges on them, amino acids, called amphoteric
IUP Intrinsically Unstructured Proteinsno defined structure under physiological conditions until they interact with other molecules
Metamorphic proteinsexist in equilibrium states with equal energies
Salt inamount of salt required to dissolve proteins in water
Salt Outamount of salt required to precipitate proteins
Specific Activitytotal activity of a protein, amount of substrate required to completely precipitate a protein
Cation Exchange ChromatographyCarboxylmethyl, negative resin sticks to positive proteins, negative proteins will elude first
Anion Exchange ChromatographyDiethylaminoethyl, positive resin sticks to negative proteins, positive proteins will elude first
Where does Chymotrypsin cleave peptides?Tyr, Trp, Phe, Leu, Met
Where does trypsin cleave peptides?Lys, Arg
Where does cyanogen bromide cleave peptides?Met
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