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Biol 141 Proteins Condensed Notes

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Comprehensive and detailed Protein Condensed Notes for Biol 141. *Essential!! *For you, at a price that's fair enough!!

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  • August 28, 2024
  • 5
  • 2020/2021
  • Class notes
  • Prof k. campbell
  • All classes
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anyiamgeorge19
 Proteins
o Amino Acids and Polymerization
 Structure
 H- hydrogen atom
 NH2- amino functional group
 COOH2- carboxyl functional group
 Distinctive R group (side chain)
 How they behave in water
 They ionize
o Causes the amino group to act as a base (forms NH3+)
o The carboxyl group acts as acid (COO+)
 Side chains
 Represents the part of the amino acid core structure that each of the 20
different amino acids unique




 Functional groups affect reactivity
o Amino acids with (SH) in the side chain can form (S-S) disulfide
bonds that help link different parts of large proteins

, o Some functional groups only have H and C atoms, which rarely
participate in chemical reactions (mean they depends primarily on
their size and shape)
 Polarity and Charge of R-groups Affect Solubility
o Hydrophilic
 Polar and electrically charged R-groups
 Dissolve easily in water
 Serine, Threonine, and Cysteine
 Acidic: aspartic acid, glutamic acid
 Basic: lysine, arginine, histidine
o Hydrophobic
 Non-polar, lack charge, highly electronegative
 Coalesce in solution
 Glycine, Alanine, and Valine
 Proline, tryptophan, phenylalanine
o 3 things to look at
 Does the R-group have – charge
 If yes, then its acidic and has lost proton
 Does the R-group have + charge
 If yes, then its basic and has accepted proton
 If the R-group has NO charge, does it have an O atom?
 If yes, then the highly electronegative O will form a
polar covalent bond, making it uncharged polar
 If NONE of the above are true
 It is a nonpolar amino acid
 How amino acids link to make proteins
o The C-N covalent bond that forms from condensation is a PEPTIDE
BOND
o Peptide bonds
 Forms in ribosomes
 Usually stable
 C-N form a double bond
 C-O single bond
 Have some of the same characteristics as double bonds
 Planar
 Limiting movement of the atoms that are in the
peptide bond
 R-group orientation
 The side chains of the residue extend to backbone,
interact with others and water
 Directionality
 Amino group on one end of the backbone and a
carboxyl group on the other
 N-terminus (amino terminus)

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