3-423-08ProteinStructure

3-423-08ProteinStructure - phobic ints X X X X Quaternary...

Info iconThis preview shows pages 1–7. Sign up to view the full content.

View Full Document Right Arrow Icon
A relatively small protein Glycine PEPTIDE BOND Condensation Hydrolysis
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
A pentapeptide: it has direction… The number of possible different polypeptides of length n amino acids?…20 n Possible dipeptides…400. Possible tripeptides…8000 Ser Gly Tyr Ala Leu Overview of protein structure
Background image of page 2
Primary structure (1 o ) -Sequence of AAs -Important bonds/ints = peptide bonds and disulfide bonds (covalent) Secondary (2 o ) -Repeating patterns -Important bonds/ints = H-bonds, vdWaals (noncovalent) Alpha helix ( α -helix) 1 4 X
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
X Constraints on α -helices: -steric interferences - too many BIG AA R-groups near each other -electrostatic interferences - several (+) charged R-groups in a row, or (-) (also possible to have attractions) -Prolines -Glycines asp arg Beta ( β ) sheets <------- Constraints on β -sheets: -Long AA R-groups not found
Background image of page 4
β -turns: -have prolines, glycines <---- Tertiary structure (3 o ) -the 3-D architecture -Important bonds/ints = hydrophobic ints, H-bonds, vdWaals (noncovalent) (Also, disulfide bonds) H-bonds, Ionic ints X<---Hydro
Background image of page 5

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 6
Background image of page 7
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: phobic ints X X X X Quaternary structure (4 o )-Only in proteins with more than one polypeptide subunit-Important bonds/ints = hydrophobic ints, H-bonds, ionic ints (mostly noncovalent) but, there are some multisubunit proteins that have covalent bonds between subunits Not all proteins have 2 o structure But there are proteins with lots of 2 o structure Ex: Collagen: skin, bone, tendon, cartilage,teeth 1 o structure = Gly every 3rd residue, lots of Pro and Hydroxyproline residues. 2 o structure = tight helix (COLLAGEN helix, not alpha) Not all proteins have 4 o structure-triple collagen helix (not )-Glycine is every 3rd residue (only one that will fit in the center of triple helix) Alterations in 1 o structure can alter final functional protein structure, function Example: Collagen-Glycine-Proline, Hydroxyproline (Scurvy, vitamin C, prolyl hydroxylase) Denaturation, renaturaton, protein folding...
View Full Document

This note was uploaded on 04/05/2008 for the course BIOCHEM 423 taught by Professor Osgood during the Spring '08 term at New Mexico.

Page1 / 7

3-423-08ProteinStructure - phobic ints X X X X Quaternary...

This preview shows document pages 1 - 7. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online