secondary structure of proteins Flashcards
secondary protein structure
regular repetitive patterns in short sections of the polypeptide chain
polypeptide chain backbone
linked by C-C and C-H single bonds which are flexible due to bond rotation
Chain flexibility
- arises from bond rotation not bond bending
- single bonds allow for rotation about bond axis
-normal 109 and 12- degree bond angles are present
conformations
state of molecule that can be interconverted by bond rotations without breaking covalent bonds
(different shapes of polypeptide chain)
configurations
can be interchanged by breaking covalent bonds, not by bond rotation
(cis and trans forms of a molecule)
X-ray diffraction
- measures repeating patterns on molecular scale
- measured in angstrom units
1 Å= 1x10^-10 meter
resonance forms of the peptide bond
one with a C-N single bond and one with a C=N double bond
- peptide bond is rigid fixing in trans-geometry because it behaves more like a double bond than a single bond
rigid planes
alpha amino and carboxylate are locked in rigid planar peptide bonds and only 2 bonds to alpha carbon can rotate freely
restricted bond rotation
limits freedom of motion so only limited structures can form - 2 possible repeating patterns
1. helical shape - every alpha-carbon turns the same direction
2. extended shape - the alpha carbon turn in alternating directions
the alpha helix
forms when amino acids all have the same orientation and alpha-carbons turn same direction
the beta sheet
strands in the same direction make parallel b-sheet
- H-bonds connect strand to strand
strands in opposite directions make antiparallel b-sheet
- H-bonds align better in antiparallel mode
amino acids preferring beta configurations
W,Y,F,V,I,T,C
- these AAs are either large, have a branch or large S atom
amino acids preferring alpha configurations
M,F,L,K,H,A,R,E,Q
- this is the default behaviour of amino acids
what determines secondary structure form
local majority of amino acids that prefer alpha or beta
secondary structure breakers
G,P,N,D,S
- disrupts secondary structure by forming a turn or loop allowing polypeptide chain to change direction up to 180 degrees
- 2 breakers in a group of 4 amino acids interrupts the secondary structure