Fichas
Lecture 2-3
Fichas del conjunto (24)
- 1Primary Structureamino acid sequence
peptide covalent bonds
-C-C-N-C-C-N- - 2Secondary Structurebackbone interactions
H-bonds of backbone where "R" groups stick out
alpha helix and beta pleated sheets - 3Tertiary StructureR group interactions - noncovalent and disulfide bonds
Folded shape of 1 polypeptide
Combination of secondary structure elements - 4Quaternary StructureR group interactions
multiple subunits linked by disulfide bridges and noncovalent bonds (hydrophobic interaction) - 5Domaindistinct modules; stable globular units
fold independently
may retain 3D structure when separated from rest of protein - 6Motifsrepetitive supersecond structure
clusters of secondary structure
beta-alpha-beta unit - 7Covalent Bondsstrong bonds
Shared electrons
Polar and nonpolar - 8Polar Covalent Bondshave partial charges
electrons are unequally shared in the molecule
hydrophilic - 9Nonpolar Covalent bondsElectron pair is shared equally in the molecule
hydrophobic - 10Noncovalent BOndsWeak, but strong in aggregate
- ionic bonds, hydrogen bonds, hydrophobic interactions, van der Waals forces - 11Ionic BondNoncovalent bond
attraction between + and (-) ions
salts - 12Hydrogen Bondsattraction of partial charges on polar molcules
- 13Hydrophobic Interactionsaggregations minimize exposure to polar molecules
- 14van der Waals Forcesattractive forces when atoms are very close
- 15Polar Charged Amino Acidshydrophilic "R" Group
fully charged
form ionic bonds
can act as acid/base
can form H-bonds - 16Polar Uncharged Amino AcidsHydrophilic "R" group
Form H-bonds and associate with water
look for electronegative atom that forms partial charges - 17Nonpolar Amino Acidmainly only carbon and hydrogen "R" group
form inner core of soluble protein
important for membrane
van der Waals and hydrophobic interactions - 18Glycinesingle hydrogen atom
Hydrophobic/hydrophilic
seen in kinks and turns of beta pleated sheets
seen in tight spaces and turns - 19Prolinehydrophobic
creates kinks - 20CysteinePolar "R" group
Forms covalent disulfide bonds b/c sulfur is outermost atom
oxidation forms bond; reduction break bond - 21HydrophilicSurface amino acids of soluble proteins are _____
- 22HydrophobicCore amino acids of soluble proteins are _____
- 23X ray Crystallographyneeds crystals
need to cleave larger proteins to see the structure
may not see the native structure - 24NMRno need for crystals
less resolution than X-ray crystallography
dynamic
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- college exam Cell Biology Fichas sobre Lecture 2-3, creado por Kayla Martinezz el 06/09/2022.
- Creado por
- Kayla Martinezz · sep 2022
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- 6 sep 2022
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