Chapter 4 Objectives

1. Two principles that contribute to the 3-D arrangement of proteins

a. Primary structure

b. Noncovalent interactions

2. Draw basic structure of a di-peptide and explain the concept of free

rotation, restricted rotation and resonance hybrids

a. Peptide unit is PLANAR

b. Peptide bond is RIGID AND HAS RESONANCE STRUCTURE

CHARACTERISTICS

c. ᾳ-CARBON-CARBOXYL and AMINO NITROGEN-ᾳ-carbon have FREE

ROTATION (about the amid unit & its 2 bonds to alpha carbon)

d. restricted rotation-limited b/w amide carbon-nitrogen bond

3. Structural features on the ᾳ-Helix

a. Stabilized by h-bonds (H-amino + O-carboxyl)

b. 3.6 aa’s per turn

c. longer

d. NO R-group form h-bonds in the helix but R-group interaction limit the
types of aa that can take part of the a-helix
 EX. Three lysines or glutamates in a row will mess up the a-helix
as will proline, which forces a turn (power)

e. Helix can wind in either direction, but only the L-aa are likely to
dance in the right-handed form

4. B-sheets

a. Fully extended

b. H-bonds can be INTRA-chain or INTER-chain

c. B-sheets are made by combining two or more regions of the

polypeptide

d. b-sheets can be in two orientations, PARALLEL or ANTI-PARALLEL

e. a.a. constraints are more sever and limited