Beruflich Dokumente
Kultur Dokumente
PROTEINS Catabolism of AA
COMPOSED OF AMINO ACIDS Characteristics:
Glycine: smallest, simplest, only aa not Amphoteric KETOGENIC
optically active, inhibitory NT, used in Optically active LEUCINE
heme syn
@low ph positively charged LYSINE
Phenylalanine: converted to tyrosine via
Phe hydrolase, associated with @high ph negatively charged
phenylketonuria GLUCOGENIC
Tyrosine: only aa with phenol grp, used in AA conversions: (13)
cathecholamine and melanin syn Histidine- histamine
(tyrosinase)
Tyrosine- melatonin, catecholamines, BOTH
Tryptophan: only aa with indole grp, used PHENYLALANINE
in the syn of 5HT/ serotonin/ happy thyroid hormone
ISOLEUCINE
hormone and melatonin Tryptophan- serotonin
TYROSINE
Histidine: histamine syn Glutamate- GABA
Arginine: converted to NO (vasodilation)
THREONINE
Arginine- Nitric oxide TRYPTOPHAN
Cysteine: aa in gluta **cystine(dimer)
Proline: no amino, has imino grp,
hydroxyproline (derivative)
CLASSIFICATION OF AMINO ACIDS Essential: PVT TIM HALL POLYPEPTIDE PRODUCTION:
Aromatic: Phe Tyr Typ Phenylalanine AMINO ACIDS LINKED BY PEPTIDE BOND
Basic: His Arg Lys Valine
Acidic: Asp A Glu A Threonine DEHYDRATION PROCESS: FORMED BET
Amidic: Asp Glu Tryptophan THE CARBOXYL AND AMINO GRP
Branched chain: Leu Iso Val Isoleucine
S containing: Cys Met Methionine LEVELS OF STRUCTURE
Alcohol cont: Ser Thr Histidine Primary: specific amino acid
Arginine sequence (left to right)
Polar: CT TAGS Leucine Secondary: spatial relation of
Cysteine Lysine
neighboring aa, hydrogen bond
Tyrosine forms helices and pleated sheets
Threonine Tertiary: spatial relation of more
Aliphatic:
Asparagine Alanine
distant residues, determine shape
Glutamate Quaternary: spatial relation
Glycine between individual polypeptide
Serine
chains in a multichain protein
Enzymes
Properties of enzymes: Enzymes Functions
Catalyze chemical reactions
1. Temperature dependent 35-40 Oxidoreductases REDOX
Governed by michaelis- menten equation
Transferases Transfer of
d. optimal 37 d. functional group
Part: 2. Ph dependent, pepsinogen
Apoenzyme: protein portion Hydrolases Hydrolytic
Co-factor: nonprotein portion
(HCl)- pepsin Isomerases Isomerization
Proenzymes/ zymogens: inactive 3. Very specific to target Ligases Join functional
enzyme *lock and key theory: groups
Plasminogen- plasmin complementary to substrate Lyases Removal of
Trypsinogen- trypsin functional groups
*induced fit theory: change
Pepsinogen- pepsin
structure to fit **ribozyme: RNA molecule that act
Fibrinogen- fibrin
Holoenzyme: apoenzyme + co-
4. Naming: prefix- substrate; asenzyme
factor: active enzyme suffix- ase
Nucleic acids DNA
DNA RNA PURINE (GuAPu) STORES GENETIC CODE
SUGAR DEOXYRIBOSE RIBOSE ADENINE STRANDS COILED AROUND HISTONE
PURINE ADENINE, ADENINE, GUANINE PROTEINS TO FORM CHROMOSOMES
GUANINE GUANINE
PYRIMIDINE THYMINE, URACIL,
PYRIMIDINE (CuTPy) B DNA-
CYTOSINE CYTOSINE
STRAND DOUBLE SINGLE CYTOSINE most common form,
THYMINE hydrated,
NUCLEOSIDE: BASE + SUGAR URACIL right handed
GUANINE +R - GUANOSINE A DNA-
ADENINE + R - ADENOSINE dehydrated,
Base pairing: connects double strand
CYTOSINE + R - CYTIDINE right handed
A-T/U: 2 H BONDS
URACIL + R - URIDINE Z DNA-
G-C : 3 H BONDS
THYMINE + D – DEOXYTHYMIDINE rare type,
left handed,
NUCLEOTIDE double stranded
B + S + PO4 (BUILDING BLOCKS OF
NUCLEIC ACIS
LEVELS OF STRUCTURAL ORGANIZATION
1. PRIMARY: UNIQUE SEQUENCE
LINKED BY PHOSPHODIESTER
BOND
2. SECONDARY: DNA DOUBLE HELIX
PROPERTIES:
COMPLEMENTARITY: (A-T/U: 2 H
BONDS
G-C : 3 H BONDS)
ANTIPARRALLELISM: STRANDS
ARRANGED IN 5’-3’
DENATURATION:H BOND CAN BE
BROKEN BY INC TEMP OR ALKALI
RENATURATIONL/ ANNEALING:
REFORM
3. TERTIARY: SUPERCOILING
(1.74 M DNA STRAND)