You are on page 1of 42

Kuliah III.

Struktur dan Fungsi

SEL: Arsitektur dan Senyawa dalam Sel

Air Karbohidrat Lipid Vitamin & Mineral Protein Asam Amino Asam Nukleat

Shape = Amino Acid Sequence

Proteins are made of 20 amino acids linked by peptide bonds Polypeptide backbone is the repeating sequence of the N-C-C-NC-C in the peptide bond The side chain or R group is not part of the backbone or the peptide bond

Polypeptide backbone

Amino Acids NOTE: You need to know this table



Struktur Asam Amino

Protein-clasified by function
Make up about 15% of the cell, have many function in the cell:
1. 2. 3.

5. 6. 7.


ENZYME : catalytic activity and function TRANSPORT : bind & carry ligands STORAGE : ovalbumin, casein CONTRACTILE (MOTOR): can contract, change shape STRUCTURAL : keratin of hair, feathers, & nails, fibroin of silk & webs DEFENSIVE (PROTECT): antibody, snake venom REGULATORY (SIGNAL): hormones RECEPTORS (DETECT STIMULI): light & rhodopsin

Protein structure
Primary structure: amino acid sequence Secondary structure: folding of single polypeptide chains

Tertiary structure: 3-dimensional shape of proteins

Quaternary structure: joining of polypeptide chains into proteins

linear sequence of peptides

each peptide is several amino acids

frequently highly folded

Peter J. Russell, iGenetics: Copyright Pearson Education, Inc., publishing as Benjamin Cummings.

Struktur Primer:

Urutan asam-asam amino yang membentuknya, terikat satu sama lain dengan ikatan peptida. The primary structure of a protein is its unique sequence of amino acids. Lysozyme, an enzyme that attacks bacteria, consists on a polypeptide chain of 129 amino acids. The precise primary structure of a protein is determined by inherited genetic information.

Protein Folding

The peptide bond allows for rotation around it and therefore the protein can fold and orient the R groups in favorable positions Weak non-covalent interactions will hold the protein in its functional shape these are weak and will take many to hold the shape

Non-covalent Bonds in Proteins

Hydrogen Bonds in Proteins

H-bonds form between 1) atoms involved in the peptide bond; 2) peptide bond atoms and R groups; 3) R groups

Protein Folding (continued)

Proteins shape is determined by the sequence of the amino acids The final shape is called the conformation and has the lowest free energy possible Denaturation is the process of unfolding the protein

Can be down with heat, pH or chemical compounds In the chemical compound, can remove and have the protein renature or refold



Dibentuk dan dipertahankan oleh ikatan hidrogen antara C=O dengan NH pada ikatan peptida Helix (3,6 asam amino), prolin (penyelang kesinambungan) Lembaran (R berganti-ganti diatas/dibawah tulang punggung).

Protein Folding

2 regular folding patterns have been identified formed between the bonds of the peptide backbone -helix protein turns like a spiral fibrous proteins (hair, nails, horns) -sheet protein folds back on itself as in a ribbon globular protein

Beta-pleated sheet

The structural properties of silk are due to beta pleated sheets. The presence of so many hydrogen bonds makes each silk fiber stronger than steel.


Core of many proteins is the sheet Form rigid structures with the Hbond Can be of 2 types Anti-parallel run in an opposite direction of its neighbor (A) Parallel run in the same direction with longer looping sections between them (B)


Formed by a H-bond between every 4th peptide bond C=O to N-H Usually in proteins that span a membrane The helix can either coil to the right or the left Can also coil around each other coiled-coil shape a framework for structural proteins such as nails and skin

Struktur Tersier Protein

Interaksi ion, hidrofobik, ikatan disulfida, ikatan kovalen Protein fibrosa (seratserat panjang, tongkat atau tali: kolagen, keratin) Protein globuler (bulat, mudah larut dalam air/garam encer): Myoglobin, ribonuclease


Protein terbanyak dalam tubuh manusia high Glycine, Proline, & no Cysteine when boiled makes gelatin 3 heliks kolagen: tropokolagen

Kolagen (lanjutan)


Keratin : kulit, rambut, kuku

high basic aa's (Arg, His, Lys), but with Cys

Membentuk serat, tongkat yang panjang dapat diregang bila basah


Keratin (lanjutan)


Keratin : sutera, paruh burung Bentuk lembaran bergelombang tidak dapat diregang bila basah

Struktur Kuarterner

Penataan suatu rantai protein dengan protein lain dan dengan koenzim, tidak terikat secara kovalen Hemoglobin, mioglobin, protein plasma, immunoglobulin, protein yang diperlukan untuk membawa Fe dan Cu

Hemoglobin & Immunoglobulin


lipoproteins (+ lipids) blood, membrane, and transport proteins glycoproteins - (+ carbohydrates) antibodies, cell surface proteins nucleoproteins - (+ nucleic acids) ribosomes & organelles

Denaturasi dan Renaturasi Protein

DENATURATION loss of 3-D conformation by heat, pH, organic solvents, detergents RENATURATION regaining of biological activity via selfassembly

Denature and Renature

Sickle cell anemia

Determinasi Struktur Protein

Molecular exclusion/gel filtration chromatography

Amino Acid Sequencing Mass Spectrometry : detects exact MASS of small peptides. X-Ray Crystallography : determines 3-D shape of molecules mathematically. NMR Spectroscopy : magnetic signal indicate distances between atoms.

The three-dimensional shapes of over 10,000 proteins have been determined using X-ray crystallograghy and NMR.



Determinasi Struktur Protein