proteins and amino acids
DESCRIPTION
Proteins and Amino Acids. Biological Functions of Proteins. Facilitate biochemical reactions Structural support Storage and Transport Immune protection Generate movement Transmission of nerve impulses Control growth and differentiation. Key Properties of Proteins. - PowerPoint PPT PresentationTRANSCRIPT
Proteins and Amino Acids
1
Biological Functions of Proteins• Facilitate biochemical reactions• Structural support• Storage and Transport• Immune protection• Generate movement• Transmission of nerve impulses• Control growth and differentiation
2
Key Properties of Proteins
• Linear polymers of amino acids• Contains a wide range of functional groups• Forms complex assemblies of more than
one polypeptide chain• Versatile structure – some are rigid while
others are flexible
3
Globular and Fibrous Proteins• Globular protein• Usually water soluble,
compact, roughly spherical
• Hydrophobic interior, hydrophilic surface
• Globular proteins include enzymes,carrier and regulatory proteins
• Fibrous protein• Provide mechanical support• Often assembled into large
cables or threads• α-Keratins: major components
of hair and nails• Collagen: major component of
tendons, skin, bones and teeth
4
General Structure of Proteins• Twenty common a-amino acids have
carboxyl and amino groups bonded to the α-carbon atom• A hydrogen atom and a side chain (R) are
also attached to the α-carbon atom
5
6
Zwitterions • Under normal cellular conditions amino
acids are zwitterions (dipolar ions):Amino group = -NH3+
Carboxyl group = -COO-
7
Stereochemistry of amino acids• 19 of the 20 common amino acids have a
chiral a-carbon atom (Gly does not)
• Threonine and isoleucine have 2 chiral carbons each (4 possible stereoisomers each)
• Mirror image pairs of amino acids are designated L (levo) and D (dextro)
• Proteins are assembled from L-amino acids (a few D-amino acids occur in nature)
8
Amino acid side chains
• Nine non-polar aa• Six polar uncharged aa• Five charged aa• Three basic aa• Two acidic aa• Two aa with sulfur groups• Four ring-forming aa• Three have aromatic rings 9
Hydropathy• Relative hydrophobicity of the
amino acid
• The larger the hydropathy, the greater the tendency of an amino acid to prefer a hydrophobic environment
• Hydropathy affects protein folding: hydrophobic side chains tend to be in the interiorhydrophilic residues tend to be on the surface
10
Acid-base chemistry of amino acids
11
Isoelectric point
12
• pH at which the amino acid bears zero net charge
Titration curve of Histidine
13
Polymer of amino acid• Peptide bond -
linkage between amino acids is a secondary amide bond
• Formed by condensation of the α-carboxyl of one amino acid with the α-amino of another amino acid (loss of H2O molecule)
14
Resonance Structure of the peptide bond
15
Trans and Cis configuration of peptide bond• Usually in the trans configuration
16
Dihedral Angle
17
Dihedral angle of proteins
• The phi angle is the angle around the -N-Cα- bond• The psi angle is the angle around the -Cα-C- bond• The omega angle is the angle around the -C1-N- bond (i.e. the
peptide bond)18
LEVELS OF PROTEIN STRUCTURE 19
Primary structure
20
>2CQG:A|PDBID|CHAIN|SEQUENCEGSSGSSGVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDSGPSSG
Secondary Structure
21
Alpha-helix
22
Right-handed and Left-handed α-Helix
23
Right-handed and Left-handed α-Helix
24
Beta-sheet
25
Determining 2o structure: Ramanchandran Plot
26
Supersecondary structure: Motifs• Secondary
structures often group together to form a specific geometric arrangements known as motifs
• Since motifs contain more than one secondary structural element, these are referred to as super secondary structures 27
Domains• stable, independently folding, compact
structural units within a protein, formed by segments of the polypeptide chain, with relative independent structure and function distinguishable from other regions and stabilized through the same kind of linkages than the tertiary level
• Often each domain has a separate function to perform for the protein, such as:• Bind a small ligand• Spanning the plasma membrane
(transmembrane proteins)• Contain the catalytic site (enzymes)• DNA-binding (in transcription factors)• Providing a surface to bind specifically to
another protein• In some (but not all) cases, each domain in a
protein is encoded by a separate exon in the gene encoding that protein.
28
Tertiary Structure
• Forces holding the tertiary (and higher order) structure together• Salt bridge• Covalent bond
(disulfide bridges)• Hydrophobic
interaction• Hydrogen bonding 29
Quaternary Structure
30
31
Protein Folding
32
33