Cataliz enzimatic.

Transport i stocare.
COMPOZITIE CHIMICA Micare coordonat.
 C  Suport mecanic.
   Imunitate.
 H 
Subst. cuaternare    P, S   Cu, Mg, Fe
 O
 
 N 
  
STRUCTURA
 macromolec ule de AMINOACIZI(50  MII)
  OLIGOPEPTI DE
PEPTIDE
 POLIPEPTID E
PROTIDE 
PROTEINE HOLOPROTEI NE
 
 HETEROPROT EINE
 
R CH COOH

NH
2
20  proteine

200 aa  α
exceptie  β alanina

1) Clasificarea aminoacizilor
din punct de vedere structural

A) AMINOACIZI ALIFATICI
a) Aminoacizi cu caten hidrocarbonat
- Glicina (Gly)
- Alanina (Ala)
- Valina (Val)
- Leucina (Leu)
- Izoleucina (Ile)
a) Aminoacizi aromatici

B) AMINOACIZI CICLICI
- Fenilalanina (Phe)

- Tirozina (Tyr)

- Triptofan (Trp)
b) Aminoacizi heterociclici
2) Clasificarea aminoacizilor
in functie de rolul biologic

a)Aminoacizi eseniali
(Thr, Met, Leu, Ile, Val, Lys, Phe, Trp)

b) Aminoacizi parial eseniali (His, Arg)

c) Aminoacizi neeseniali (restul)

H CH COOH

NH2
glicina

(acid - aminoacetic)
ROL -structura gelatinei i fibroinei (25%, 40%);
-compoziia acizilor biliari, glutationului,
-particip la sinteza de purine i de porfirine;
-participa la eliminarea nucleului benzenic sub forma de
acid hipuric
(C6H5-CO-NH-CH2-COOH

CH2 COOH CH2 COOH

+
NH N

CH3 H3C CH3 CH3

monometil-glicina trimetil-glicina
(sarcozina) (betaina)
Surse de grupari –CH3
 H3C CH COOH CH2 CH2 COOH

NH2 NH2
a - alanina  - alanina
(acidul -amino-propionic)

 aa neproteic

 
 
acid pantotenic
ROL  
  intra in compozitia coenzima A
 
 carnozina
 dipeptide musculare
  anserina
 (aa esenial)

CH3 CH CH COOH
CH3 NH2

valina

(acidul -amino-izovalerianic)
 (aa esenial)

CH3 CH CH2 CH COOH

CH3 NH2

leucina

(acidul -amino-izocaproic)
 (aa esenial)

CH3 CH2 CH CH COOH

CH3 NH2

izoleucina

(acidul -amino--metil valerianic)

 CH2 CH COOH

CH2 CH COOH O
NH2

NH2 OH P O
OH
OH
serina
fosfoserina
(acidul -amino--hidroxi-propionic)
 (aa esenial)

CH3 CH CH COOH

OH NH2

treonina

(acidul -amino--hidroxi-butiric)
 CH2 CH COOH

SH NH2

cisteina

(acidul -amino--mercapto-propionic)
 CH2 CH COOH CH2 CH COOH
2
SH NH2 S NH2
+ 2H+ + 2e-
cisteina S
CH2 CH COOH

NH2

cistina
Oxidare avansata ac. cistic  TAURINA  ac .biliari
CO 2
 
Decarboxilare  CISTEAMINA(CoenzimaA ) 
HS - CH2 - CH2 - NH2

Cisteamina

(aa esenial)

CH2 CH2 CH COOH

surs de metil
S NH2

CH3
metionina(acidul -amino--metil-mercaptobutiric)
HOOC CH2 CH COOH CO CH2 CH COOH

NH2 NH2 NH2

acid aspartic
asparagina

(acidul -amino succinic)

HOOC CH2 CH2 CH COOH

NH2

acid glutamic

(acidul -amino-glutaric)
 OC CH2 CH2 CH COOH

NH2 NH2

glutamina

ROL
Transportarea   ASPARAGINA  vegetale
  AZOT AMINIC 
Depozitare a  GLUTAMINA  animale
e d g b a
CH CH2 CH2 CH2 CH COOH
2
NH2 NH2

lizina

(acidul ,-diamino-caproic)
CH2 CH CH2 CH2 CH COOH

NH2 OH NH2
4-hidroxi-lizina

ROL
 Aa. esential 
 
 GELATINA
 Hidroxi  lizina   COLAGEN 
COMPOZITIA

  
 d g b a
NH2 C NH CH2 CH2 CH2 CH COOH

NH NH2

arginina
(acidul -amino--guadin-valerianic)
ROL


 Aa .partial esential

CICLUL UREOGENETIC

Compozitia proteine BAZICEHISTONE
 PROTAMINE
 ROL
b a
 COPII
CH2 CH COOH  Aa. esential 
  ANIMALE
N NH Compozitie GLOBULINE
NH2 
histidina

(acidul -amino--imidazol-propionic)

(imidazol-alanina)
 (aa esenial)

b a
CH2 CH COOH

NH2
fenilalanina
(acidul -amino--fenil-propionic)
 b a
OH CH2 CH COOH

NH2
tirozina

(acidul -amino--(para-hidroxi-fenil)-propionic)
 (aa esenial)

b a
CH2 CH COOH

N NH2
H
triptofan

(acidul -amino--indol-propionic)
(indol-alanin)
ROL
max. absorbtie LUV λ  280

 Tyr    xantoprote ica
    
 Trp  pozitiveaz a reactii  Millon
  Adamkiewicz
 
hormoni tiroidieni (tiroxina)

 dopamina
 Tyr   
   precursoricatecolami ne epinefrina
 Phe   norepinefr ina
 
pigmenti melaninici
 N COOH
H
prolina

(acidul pirolidin-2-carboxilic)
 OH
N COOH
H
hidroxi-prolina

ROL
 Aa. cu functia aminica secundara (AA. SUBSTITUITI)

 Aa. predominanti in str.COLAGEN (dupa glicina)
 condensare a  aa2  100   leg. PEPTIDICA 

Subst. nat.        
Cys - NH - CO - lys - NH - CO - glu 
 
Subst. macromolec ulare; n  mic; MONOMER  AMINOACID

 dipeptide (2 aa)

OLIGOPEPTIDE ( 10 aa)  tripeptide (3 aa)
PEPTIDE  tetrapeptide (4 aa)
POLIPEPTIDE (10  100 aa) 
 pentapeptide
Oligo
 hexapeptide
 heptapeptide

 octapeptide
 nonapeptide (9 aa)

1) pept. liniare 
 
2) pept. ramificate 
 
3) pept. ciclice 
4) pept. semiciclice
 

 prezenta  CO  NH  ;
 secventa de aminoacizi
  COOH 
 
  NH 
 prezenta gr.  2  libere
  OH 
 
  SH 
 
H2N CH COOH + H2N CH COOH

R1 R2
H2O
aa 1 aa 2

H2N CH COOH

R3
H2N CH CO NH CH COOH

R1 R2
H2O
dipeptida
 (n-3) aminoacizi
H2N CH CO NH CH CO NH CH COOH

R1 R2 R3 H2O

tripeptida

H2N CH CO NH CH CO NH CH COOH

R1 Ri n-2 Rn

polipeptida
i = 2,3......n-2
 Rest de aa " il"denumirea completa aa final 
 
 Exemplu : 
 tyr  ala  val  leu  cis  trp 
 
 tirozil  alanil  valil  leucil  cisteinil  triptofan 
 



1) caracter AMFOTER

 2) solubilitate HOH

  ACIDA 
   aa
 3)HIDROLIZ A  
  ENZIMATICA (peptidaze ) 
4) Reactia BIURETULUI

NH2
O=C NH2
NH2 O=C CuSO4
NH
NH2 - NH3 2 NaOH
O=C O=C
NH2 NH2
uree biuret
-2
O H H O

C N N C
HN Cu NH 2 Na+
C N N C

O H H O
complex cuproalcalinic
(culoare violet)
HOOC CH CH2 CH2 CO NH CH CO NH CH2 COOH
NH2 CH2 SH
GLUTATION

( GAMMA-glutamil-cisteinil-glicina)
HOOC CH CH2 CH2 COOH + NH2 CH COOH + NH2 CH H
NH2
CH2 SH COOH
acid glutamic cisteina glicina 2 H2O

HOOC CH CH2 CH2 CO NH CH CO NH CH2 COOH

NH2 CH2 SH
glutation redus
( GAMMA-glutamil-cisteinil-glicina)

-legtur peptidoid
2 HOOC CH CH2 CH2 CO NH CH CO NH CH2 COOH
NH2 CH2 SH - 2 H+ - 2e-
glutation redus

HOOC CH CH2 CH2 CO NH CH CO NH CH2 COOH

NH2 CH2
S
S
CH2
HOOC CH CH2 CH2 CO NH CH CO NH CH2 COOH
NH2
glutation oxidat
- particip la reaciile redox celulare conform reaciei

-2 H
2G-SH G-S-S-G
+2 H
glutation glutation
redus oxidat

- joac rol de coenzim( donor de H):

A + 2 G-SH AH2 + G-S-S-G

ox1 red2 red1 ox2
 activeaza enzime  SH dependente
Oxigen singlet ( 1 O 2 )
 .
Superoxid (O 2 )
 actioneaza ca antioxidant (RLO 2  2
 Peroxidul de hidrogen (O 2 )
R. hidroxil (OH . )

xenobiotice
 participa la detoxifiere
deseuri metabolice

 FAZA aII  a de DETOXIFIER E 

 
  conjugarea cu G  SH  GLUTATIONO  CONJUGATI( solubili) 
 
  cataliza enzimatica  GLUTATION  S  CONJUGAZA 
Nonapeptide secretate de lobul posterior al HIPOFIZEI
 1 2 3 4 5 6 7 8 9
H2N - Cys -Tyr - Ile - Gln - Asn - Cys - Pro - Leu - Gly - CONH2

S S
Ocitocina

H2N - Cys -Tyr - Phe - Gln - Asn - Cys - Pro - Arg - Gly - CONH2
sau Lys
S S
Vasopresina
Caracteris tici
 Deosebiri structural e

 pozitia 3 : Ile INLOCUIRE
  Phe

 pozitia 8 : Leu INLOCUIRE  Arg
  
 Lys

 Deosebiri functiona le

 contractia musc. uterine
 Ocitocina   lactatia
STIMULAREA

  
 hipertensiv (contr. vaselor)
  Vasopresin a   
ACTIONEAZA

 antidiuretic
  secretat de hipofiza anterioara



  compozitie : 39 aa24 aa  secv. invariabil a(  functia biolologic a)
 15 aa  secv. variabila


  Functia : STIMULA SECRETIADE H. STEROIZI

  corticosup rarenala








  secretat de pancreas

 Functie : H. HIPOGLICEM IANT
 6000 (monomer)
 
 12000 (dimer)
 MM : 
 24000 (tetramer)
 48000 (octamer)

 Structura

 catena A  21aa  aa bazici
 1punte S  S (cys6  cys11)

 catena B  30 aa  aa bazici
 cys7(A)  cys7(B)
  2punti S  S intre A si B
 cys20(A)  cys19(B)

Caracteris tici


  secretat de pancreas

 Structura29 aa
 
unica

 antogonist al insulinei
 Functie 
 HIPERGLICEMIANT
        
 structura primara
 structura sec undara LEGATURI
 str. primara: leg. peptidica (secv. de aa)

 structura tertiara  
a) leg. peptidica
 
 b) leg.disulf hidrica
 structura cuaternara 



  str. secundarab) leg.ionica
 
 c) leg.de hidrogen
 
 d) leg.hidrof oba
Ca Ca H
H +
C N C N
-O
O Ca ' Ca '
Ca H
C N
O Ca '

Ca H
+
C N
- O Ca '
CARACTERISTICELE LEG. PEPTIDICE
 Cα 
  
 C 
  O   coplanari
  implica
 
 H 
  
 C
 α' 
  izomerie cis  trans (C siC ) in raport C  N
 α α'

  forma TRANS  proteine naturale








3 posibiliti de dispunere spaial a planurilor formate
prin legturi peptidice succesive ale unei catene peptidice

1) Planurile succesive alterneaz unul fa de

altul conform a dou orientri spaiale
privilegiate => structura "n foi plisate“
(structur de tip periodic);

2) Planurile succesive se rotesc regulat,

totdeauna n acelai sens unul n raport cu
cellalt => structura de "form helicoidal"
(structur de tip periodic);
3) Planurile se pot roti la ntmplare unul fa de
altul => structura "n ghem statistic"
(structur de tip neperiodic).
 O

C
R 4
H 3 N

H
N
H O
C

2 C
R N 1
H
H
Structura teriar a globinei din mioglobin
Structura cuaternar a colagenului, protein fibrilar cu rol de susinere.Lungile catene
polipeptidice ale colagenului sunt dispuse sub form de triplu helix. Structura cuaternar
a hemoglobinei, protein globular,ce comport 4 catene polipeptidice i 4 molecule de
hem. Oxigenul se ataeaz la structura hemoglobinei prin fierul hemului.
Masa moleculara
MM  mii  miloane daltoni
 24
1dalton  1,67x10 g (MM atom H)

Insulina (MM = 6.000);

Ribonucleaza (MM = 13.700);
Ureaza (MM = 480.000)
Solubilitatea

  proteine solb .in apa; 

 
  proteine solb .in sol de electroliti;
 
  proteine solb in sol acide; 
 
  proteine solb in sol alcaline; 
 
  proteine complet insolb . 
 
Denaturarea
 caldura
 radiatii UV si ionizante
Agenti de denaturare  acizii
 solv .org.
 urea si guanidina
 
 
 
 
  dezorganizarea str. spatiale 
Definitie   nu este afectata str. primara 
 
  leg. S  S  
  consecinta disparitiei leg. de H  
  
  leg. ionica  
  
Denaturarea reversibil a ribonucleazei
REPERCUSIUNILE DENATURARII



 pierderea activitatii biologice

 diminuarea solubilitatii

 pierderea capacitatii de hidratare
 aparitia de noi grupari functional e

  vascozitate
 
 modificare reactii de culoare
 presiune osmotica
 
Caracter coloidal
n sol. diluate =>coloii hidrofili (1-100 m)
n sol. concentrate => micele
CONSECINTA: nu dializeaza prin membrane

Caracter amfoter
pH=1 pH=7 pH=11
+ +
H3N PROTEINA COOH H3N PROTEINA COO - H2N PROTEINA COO- + H+

cation zwiterion anion

Punct izoelectric (pHi)

 pH i [pep sin a]  1 
 
 pH i [Hb]  6,9  =>separarea, purificarea proteinelor
 citocrom  10,6 
 c 
PROTEINE FIBROASE
 fibroina 
 
scleroprot eine  colagen (tes.conju nctiv, tendoane) 
 keratina (piele, fanere) 

PROTEINE GLOBULARE
 albumine 
sferoprote ine  
 globuline 
1)Albumine
2)Globulin e
3)Protamin e, histone
4)Globine
5)Prolamin e, gluteline
6)Scleropr oteine
a) miozina

b) actina
7)Prot.fib rilare
c) troponina
d) tropomiozi na

 HOLOPROTEI NE : (aa)n 
 
  fosfoproteine 
  glicoproteine 
 
  
 HETEROPROT EINE  lipoproteine 
  nucleoproteine
  
  cromoproteine 
Definitie  Fe

proteine colorate; gruparea prost.  Cu
 Mg


Clasificarea
cromoproteinelor

 str. porfirinica, neporfirinica

 
 rol respirator, nerespirator 
 
  
 
  Hemoglobin e
   Citocrom a (hem a )
 
 Pigm. respir (Fe) .  Citocromi  Ctocrom b (hem b )

 Cr. porfir.    Citocrom (hem )
   c c

   Peroxidaze
  Enzime hemininice 
   Catalaze

 Pigm. nerespir Cloroplast ine [clorofila ](Mg)
   Hemiretrin e (Fe)
Pigm.respi r. 
  Hemocianin e (Cu)

 
 
   αc aroten
  Carotenopr oteine  βc aroten
  
 Cr. neporfir    vit.A
 
 Pigm.neres pir.  Flavoprote ine
 
   Feritina
   Fe 
    Siderofili na
  Metaloprot eine 
   Cu Hemocuprei na
   
    Ceruloplasmina
Hb = HEM(4%) + GLOBINA(96%)

HEM = protoporfirin + fier

4 nuclee pirolice + =CH- PORFINA

substituti a H(8) de la C

PORFINA            PORFIRINE
 PORFINA 

substituti e cu CH COOH, CH CH COOH

         2  2 
2 


 UROPORFIRI NA

PORFIRINE  metale (Fe, Co, Mg , Mn )  METALOPORF IRINE

PORFIRINE  Fe  2  HEMI
Exceptie : PROTOHEM (PROTOPORFIRINA)
PORFIRINE  Fe  3  HEMATINE
 H H
Atomi de carbon si '
1 2
HC I
CH
N
H 8 H
7
IV N HN II 3
4
Atomi de carbon si  '
H H H
N
HC III CH
6 5

H H
Structura porfinei
 CH2
CH3 CH

1 2
 I 
N
CH3 8 CH3
IV N HN II
3
4
7
HOOC CH2 CH2 H CH CH2
N
 
III
6 5

CH2 CH
3
CH2

COOH
Structura PROTOPORFIRINEI
  varsta

Globina = compon. proteic (struct.variaza  specia )

 st. patologica

Mioglobina globina  1 catena polipeptid ica

2(141 aa)
Hemoglobin a globina  4 catene polipeptid ice  4 HEM 
(146 aa) 

2 (141 aa)

Hb.FETALA globina  4 catenepolipeptidice   4 HEM
2 (131 aa) 

A
HbA  α2 β2A
HbF  α2A γF2
  Hb.P   A
 4
 repartitie de catene Ex :  
 Hb.P   A
 4
 catena 
Hb.P  anomalie de secventa
 catena 
catena 
      
Ex : glu (6)  val (6)  anemia falciforma
          
 1) Combinarea cu oxigenul = oxihemoglobina

Hb  4  4O 2  HbO 2  4 (oxihemogl obina)

2) Combinarea cu CO = carboxihemoglobina

[Hb]4  4CO  [Hb  CO]4

3) Combinarea cu CO2 = carbhemoglobina

Proteine sanguine  CO 2  CARBAMINOP ROTEINE

CO 2  Pr oteina  NH 2  Pr oteina  NH  CO  OH

4) Oxidarea reversibila a Hb = METHEMOGLOBINA

Hb(Fe 2 )  Oxidant(fe ricianura ) 

METHEMOGLOBINA(Fe 3 )  reducator( ferocianur a)