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tyrosine
10.1
cystine
8.2
lysine
10.5
histidine
6
arginine
12.5
glutamic acid
4.2
aspartic acid
3.6
carboxylic group
2.2
amino grup
9.4
6a
overall shape,helices as rods, sheets can be seen but not individual strands
3.5 A
Trace the backbone (3.5 < 5.4 Å for helix and <5Å between strands in sheet ; bulky side chains visible
2-2.5A
Side-chain shapes; similarly shaped side chains assigned using the protein 1 ̊ structure
1.5A
Atom shapes start to separate (C–C bond ≈ 1.5 Å)
1.2A
Individual atom positions
where does the a helix singal in the circular dichroism
two minima 208 and 222 nm peak at 195 nm , range 20 to -15
what B sheets signal in the circular dichromsm
one minimum 216-218 nm, and max at 195nm , 10 to -10
where does unstructed signal in the circular dichroism
mimumunm near 198 nm -5 to -0 , flat at 0 at 210
what amino acids favor helix
Glu, Met, Ala, Leu
what amino acids favor strand
Val, Ile, Tyr, Phe, Trp, Thr
what amino acids favor turn
Gly, Pro, Asn, Asp, Ser
where do you see antiparallel beta sheets in ramchandran diagram
phi=-139, psi=+135
where do you see parallel beta sheets in ramchandran diagram
phi=-119, psi=+113
where do you see left handed alpha helix in ramchandran diagram
phi=+57 , psi=+47
where do you see right handed alpha helix in ramchandran diagram
phi= -57, psi= -47
cofactor
non-protein chemical compound or metallic ion required for a protein—usually an enzyme—to function correctly