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Important biological functions of proteins 1. Enzymes, the biochemical catalysts 2. Storage and transport of biochemical molecules
Globular proteins
Usually water soluble, compact, roughly spherical
Hydrophobic interior, hydrophilic surface
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Fibrous proteins
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Optical Activity
L D
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Formation of cystine
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Basic Lys Arg His Polar Charged Lys Arg Glu Asp His Non-polar Gly Ala
Prentice Hall c2002
Leu Ile
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Val
Met
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Ionization of Histidine
(a) Titration curve of histidine pK1 = 1.8 pK2 = 6.0 pK3 = 9.3
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Peptide chains are numbered from the N (amino) terminus to the C (carboxyl) terminus
Example: (N) Gly-Arg-Phe-Ala-Lys (C) (or GRFAK) Formation of peptide bonds eliminates the ionizable a-carboxyl and a-amino groups of the free amino acids
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Secondary structure - regions of regularly repeating conformations of the peptide chain, such as a-helices and b-sheets Tertiary structure - describes the shape of the fully folded polypeptide chain
Quaternary structure - arrangement of two or more polypeptide chains into multisubunit molecule
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a-helix
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Common motifs
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Quaternary Structure
Refers to the organization of subunits in a protein with multiple subunits (an oligomer) Subunits (may be identical or different) have a defined stoichiometry and arrangement
Subunits are held together by many weak, noncovalent interactions (hydrophobic, electrostatic)
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Hemoglobin tetramer
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