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- author "FatNerdd"
- tags "Amino acids, proteins, organic, chemistry, Handedness, structure"
- description "Chapter 18 - Amino Acids and Proteins
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Textbook: Fundamentals of General, Organic, and Biological Chemistry Volume 2 by McMurry, Castellion, Ballantine, Hoeger, and Peterson.
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- fileName "Organic Chemistry Ch. 18"
- freezingBlueDBID -1.0
- Primary Structure of Protein
- The sequence of amino acids ina protein chain (ch. 18.7)
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Secondary Structure of Protein
The regular and repeating spatial organization of neighboring segments of single protein chains ( ch. 18.9)
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Tertiary Structure of Protein
The overall shape of a protein molecule (ch. 18.10) produced by regions of secondary structure combined with the overall bending and folding of the protein chain.
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Quaternary Structure of Protein
Refers to the overall structure of proteins composed of more than one polypeptide chain (ch 18.11).
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Noncovalent Forces
Forces of attraction other than covalent bonds that can act between molecules or within molecules
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Zwitterion
A neutral dipolar ion that has one + charge and one - charge
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In what ways are the physical properties of amino acids and salts similar?
Pure amino acids can form crystals, have high melting points, and are soluble in water but not in hydrocarbon solvents.
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Amino acid zwitterions in acidic solution (low pH)
Amino acid zwitterions accept protons on their basic --COO- groups to leave only the positively charged --NH3+ groups.
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Amino acid zwitterions in basic solution (high pH).
Amino acid zwitterions lose protons from their acidic --NH3+ groups to leave only the negatively charged --COO- groups.
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Enantiomers (Optical Isomers)
The twwo mirror-image forms of a chiral molecule
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Stereoisomers
Isomers that have the same molecular and structural formulas but different spatial arrangements of their atoms
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