AMINOACIZI SI PROTEINE

CURS 2

PROTEINE
- STRUCTURA SI FUNCTII-

Functiile proteinelor
Componente structurale ale proteinelor
Sursa de energie
Enzime
Anticorpi
Hormoni
Mentinerea presiunii coloid osmotice
Transportor (O2, acizi grasi, medicamente,
compusi toxici pentru organism)

Structura proteinelor

Structura proteinelor-legaturi
Legaturi peptidice
Legaturi de hidrogen
Punti de sulf
Legaturi ionice
Forte hidrofobe

Tabel comparativ
Structura

Definitie, caracteristici

Tipuri de legaturi

Primara

Secventa de aminoacizi

Legaturi covalente

Secundara

Structuri repetitive realizate prin legaturi de

hidrogen intre carbonilul dintr-o legatura
peptidica si NH dintr-o alta legatura
peptidica
PERIODICITATEA

Legaturi de hidrogen

Tertiara

Conformatie tridimensionala realizata din

legaturi stabilite intre radicalii R ai
aminoacizilor

Legaturi de hidrogen
Legaturi ionice
Interactii hidrofobe
Punti disulfurice

Cuaternara

Aranjamentul spatial al subunitatilor intr-o

proteina formata din cel putin doua lanturi
polipeptidice

Legaturi de hidrogen
Legaturi ionice
Interactii hidrofobe
Punti disulfurice

Structura primara a proteinelor

Primary structure of insulin

Bettelheim & March (1990) Introduction

to Organic & Biochemistry
(International Edition) Philadelphia:
Saunders College Publishing, p299

STRUCTURA PRIMARA
Precizeaza numarul, tipul si secventa resturilor
aminoacidice
Numita si structura covalenta
Este esentiala pentru intelegerea functiilor
proteinei
Codificata genetic
Structura unica
substitutii conservative si neconservative (poate
altera mult funcia proteinei).
Polimorfism molecular (poate exista sub forme
moleculare diferite)

Structura primara anormala

Inlocuirea unui
singur glu cu val intrun singur lant

polipeptidic al Hb
duce la alterarea
structurii si functiei
(se formeaza HbSsiclemie)

Bettelheim & March (1990) Introduction to Organic & Biochemistry

(International Edition) Philadelphia: Saunders College Publishing, p301

Structura secundara a proteinelor

Sunt doua tipuri de structuri
secundare:
- helix
- foaie plisata

- helix
Pauling Corey1951
Structura spiralata
realizata prin legaturi de
hidrogen intre grupele
C=O si N-H din strucura
primara
Legatura se realizeaza
intre oxigenul unui rest
carbonil si hidrogenul unui
rest amidic de la cel de-al
4-lea aminoacid
Helixul se roteste spre
dreapta
Radicalii R se afla
perpendicular si in afara
axului structurii secundare

 - helix
0.54nm pitch
(3.6 residues)
Hydrogen
bonds parallel
with helix axis

Side chains R
located
outside the
helix

Diameter 10-12 A

-helix
Intrerupt de:
- resturile de Pro
- resturile de Gly
- regiuni formate din
aminoacizi cu grupe polare
incarcate(eg. Asp, Glu, Lys,
Arg), sau radicali hidrofobi
mari (Leu, Ile, Trp, etc.)

Structura mioglobinei

 - foaie plisata
Structura realizata
din legaturi de
hidrogen intre
grupele C=O si N-H
dintre doua lanturi
polipeptidice sau
dintre doua regiuni
ale unui singur lant
polipeptidic
Radicalii R se afla
dispusi deasupra si
dedesubtul structurii
From: Elliott, WH. Elliott, DC. (1997) Biochemistry and Molecular
Biology. Oxford: Oxford University Press. p29

 - pleated sheet

Lanturi antiparalele

Lanturi paralele

Structura tertiara
Se realizeaza prin interactii intre radicalii
aminoacizilor dispusi perpendicular pe
structura secundara

Tertiary Structure

Tertiary structure 1) H bond

H bonds weak
allowing to be
broken and
reformed easily
Allows structural
change
produces
functional
molecules

Tertiary structure 1) H bond

Hydrogen bond

H bonds weak
allowing to be
broken and
reformed easily
Allows structural
change
produces
functional
molecules

Tertiary structure 2) ionic bond

Ions on R
groups form
salt bridges
through ionic
bonds
From: Summerlin, LR. (1981) Chemistry for the Life Sciences. New
York: Random House, p459

Tertiary structure
3) hydrophobic forces
Close attraction of nonpolar R groups through
dispersion forces
Very weak but collective
interactions over large
area stabilise structure
Repel polar and charged
molecules/particles

Bettelheim & March (1990) Introduction to Organic & Biochemistry

(International Edition) Philadelphia: Saunders College Publishing, p302

Tertiary structure
4) disulfide bond
Covalent bond
between sulfur
atoms on two
cysteine amino
acids

From: Elliott, WH. Elliott, DC. (1997) Biochemistry

and Molecular Biology. Oxford: Oxford University
Press. p32

Quaternary protein structure

Arrangement of multiple tertiary
structures into single functional
complex
Only in multimeric proteins
(with multiple polypeptide
chains)
Chains can be identical eg
homeodimer or different eg
heterodimer
Allows for changes in
structure/function in response
to chemical stimuli
From: Elliott, WH. Elliott, DC. (1997) Biochemistry and
Molecular Biology. Oxford: Oxford University Press. p27

Quaternary structure
Example:
Hemoglobine
4 chains
22

8 -helix regions in each chain

Non-polar aa are in the interior and
the charged aa are on the surface

Properties of proteins
Solubility- fibrous proteins are insoluble in
water, globular proteins are usually soluble
(excepting membrane proteins)
Isoelectric pH
Denaturation (destruction of secondary,
tertiary and quaternary structures)
Renaturation (returning to the native state
after the denaturing agents is removed)

Denaturation

Renaturation

Classification of proteins
Proteine plasmatice
Hemoproteine