HTHSCI 1LL3 Lecture Notes - Lecture 5: Adrenergic Receptor, Blood Sugar, Cell Surface Receptor
22 Jun 2018
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STRUCTURE AND FUNCTION
IN PROTEINS
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§EUUCCIIEE DaE
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protein Structure
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The conformation Ior shape)of aprotein predicts its function -proteins held in their shape mostly by non covalent bonds
•There are several different general types of structure for proteins
•Globular proteins 1hemoglobin ),throw proteins (collagen ),transmembrane PWKMJ ,and DNA binding proteins are major classifications for the
different types
Levels of Structure
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Primary Structure :sequence of a chain of amino acids
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Secondary Structure :hydrogen bonding of the peptide backbone causes amino acids to fold
into arepeating pattern
lnheliasorpaeated
sheets )
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Tertiary Structure :3D folding pattern of aprotein due to side chain interactions
-Quaternary
Structure :protein consisting of more than one amino acid chain
>eg .hemoglobin
>vote in Structure Rules
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The 317 structure must be flexible enough to function properly but stable enough that it will not convert to another conformation
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It must have amino acids with side groups that are compatible with the environment or environments Itransmembrane protein )the protein
will function in
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.:Polar groups on the outer surface if it will function in aqueous environments ,hydrophobic groups in membrane insertion areas it it is a
transmembrane protein
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Peptide Bonds :bonds that form the backbone of proteins is that between an amino group and a carboxyl group
Water is ejected ,charge is lost on individual amino ands ,and bond is formed
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Partial double bond characteristics allow the bond to be fairly rigid
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The R-
groups are usually on opposite sides of the bond
aHelices
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Common secondary structure
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It is aregular repeating structure where the coil is maintained by Hbonds between the H in the N-H
bond and the 0of the carbonyl group 4aa 's away
Document Summary
I or shape) of a protein predicts its function proteins held in their shape mostly by non covalent bonds. There are several different general types of structure for proteins. Globular proteins 1 hemoglobin ) throw proteins ( collagen ) transmembrane. Pwkmj , and dna binding proteins are major classifications for the different types. Primary structure : sequence of a chain of amino acids a repeating pattern the peptide backbone. Tertiary structure : 3d folding pattern of a protein due. Structure : protein consisting of more interactions sheets ) to side causes chain one amino acid chain than amino acids to fold into eg . hemoglobin. The 317 structure must be flexible enough to function properly but stable enough that it will not convert to another conformation. It must have amino acids with side groups that are compatible with the environment or environments. I transmembrane protein ) the protein will function in.
