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BAHAN KULIAH BIOKIMIA POWER POINT BAGIAN 1 /BIOCHEMISTRY POWER POINT LECTURES PART 1 | Karya Tulis Ilmiah

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(1)

Protein Structure

(2)

beta sheets are twisted

• Parallel sheets are less twisted than antiparallel and are always buried.

(3)

The twist is due to chiral (l)- amino acids in the

extended plane.

This chirality gives the twist and distorts

H-bonding.

(4)
(5)

Two proteins exhibiting a twisting



sheet

Bovine carboxypeptidase

(6)
(7)

Sheet facts

Repeat distance is 7.0 Å

R group on the Amino acids alternate up-down-up above and below the plane of the sheet

2 - 15 amino acids residues long

2 - 15 strands per sheet

Ave of 6 strands with a width of 25 Å

parallel less stable than anti-parallel

Anti-parallel needs a hairpin turn

(8)

Non-repetitive regions

Turns - coils or loops link regions of secondary structure 50% of structure of globular proteins are not

repeating structures

bends

(9)
(10)
(11)
(12)

Folding motifs (super secondary

structure)

Certain amino sequences have patterns to their folding.

A.  motif, B.  hairpin C.  motif

(13)

beta-alpha-beta

• parallel beta-strands connected by longer regions containing alpha-helical segments

(14)

Helix-turn-helix

• loop regions connecting alpha-helical segments can have important functions e.g. EF-hand and DNA-binding

• EF hand loop ~ 12 residues

• polar and hydrophobic a.a. conserved positions • Glycine is invariant at the sixth position

(15)

Protein Folds

There is an estimate of about 10000 different folding

patterns in proteins

About half of the proteins fall into a few dozen folding

patterns.

(16)

The  barrel has several types of

structures that have been mimicked in art.

A. rubredoxin

B. Human prealbumin or porins

(17)

Concanavalin A

(18)

Carbonic anhydrase

H

2

CO

3 -

CO

(19)
(20)

Glyceraldehyde-3-phosphate

dehydrogenase

(21)

Zinc fingers

C2H2 zinc finger: It is characterized by the sequence CX2-4C....HX2-4H,

where C = cysteine, H = histidine, X = any amino acid.

C4 zinc finger: Its consensus sequence is CX2CX13CX2CX

14-15CX5CX9CX2C. The first four cysteine residues bind to a zinc ion and

the last four cysteine residues bind to another zinc ion

C6 zinc finger. It has the consensus sequence CX2CX6CX5-6CX2CX6C.

(22)
(23)
(24)

Summary Chapter 6

• Four levels of protein structure

– Primary

• Tertiary structure (fibrous or globular)

• Structure determination and fold space

Referensi

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