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THEORY OF THE PROTEIN FRAGMENTS
DIMOSTHENIS A. ADAMIDIS
commissary A KYK 2006-01-21
At the duration of mitosis process evolve a line of biochemical activities included and
this process of doubling of DNA as well as the protein composition is increased as
is completed in the telofasis while reopen the membranal circulation endocitosis and
the exocitosis. Each affiliated cell is found now in phase G1 of next mesophasis. The
mesophasis begins as the cell from a previous cellular division it enters in a phase of
increase. Τhis period be composed of proteins and other cellular molecules but
is observed also the copy of DNA. This phase is named G1 (Gap = gap it is reported
in the not copy of DNA in this particular phase). In some point and provided that the
cell is to be divided it begins the copy of DNA. The beginning of copy of DNA
signals the end phase G1 and the beginning of phase S (S = DNA composition).At the
phase S redoubling with big precision entire the nuclear DNA. In each cellular circle
the DNA should be copied only one time.This is achieved not with mechanisms of
retroaction but with a system self-restraint of copyv each department of chromatin as
soon as it is copied it is altered with a such way so that it impedes his copy
for second time at the duration of same cellular circle.New copy is impeded because
the connection of protein or some other molecule in the concatenations of DNA
immediately afterwards his copy in the phase S. At the mitosis the factor of hindrance
is removed. As is completed the copy of DNA the phase S finishes also the cell it
enters in the final stage of mesophasis phase G2. Most cellular types remain in phase
G2 for very small time interval.In the end of phase G2 that signals the expiry of
mesophasis and the begins of mitosis. Each stage of mesophasis is characterized from
particular model of cellular composition. At phase G1 substantially be composed of
all the proteins the carbohydrates and the lipids where it is characteristically for each
cellular type but does not become a copy of the DNA. Despite make that the
constitution of all teams cellular macroaggregated it is also continued at the phase S
and G2 the phase S it is characterized by the copy of DNA and the composition of
histons and the not histons proteins.Phase G2 is characterized by the composition
team of proteins that is essential for the entry of cell in mitosis. To the end of phase
G1 and provided that the cell it is divided are activated the genes for the beginning of
copy of DNA.
From the moment where will begin the phase S the cellular division segue without
disturbances. Substantially the molecular switches that activate phase S they activate
also the remainder stages of cellular circle in more cells. The critical time period in
the end of phase G1 is activated the phase S is named beginning in inferior Eukaryotic
cells and point of restriction (restriction point) or point of control G1 (G1 checkpoint)
in the superior eukaryotic cells. Other factors that influence or regulate the cellular
circle include changes in the transport of ions via means of cellular membrane change
in the pH modifications in histons and in not histons proteins and changes in the
stocking of polyamines a team of small basic molecules (addition of polyamines it
accelerates the copy of DNA and the cellular division). In most eukaryotic cells the
changes in the upwards factors they constitute part of chain reactions that are caused
by membranal receptor. In many cases we dont known the way which this factors they
modify the regulation of cellular circle. It believes that the regulation it is achieved
immediately or indirectly
A. with the activation or deactivation genes of cellular circle and
B. with the excitation or hindrance products of this genes.The activation and the
deactivation of these genes it is realised by commands that are transmitted in cell via
means of proteins that are produced by them.Today the scientists believe that the
creation of cancer cells is owed to the gene mutation of healthy cells. My theory
believes and will try to prove that no gene mutation happens to the cancer cells and
the only responsible in charge for the cancer situation of cells are the ferments and in
particular concrete ferments that determine the production of defective proteins.
Let’s think what happens at the doubling of DNA one double helix which is unfolded
and each chain functions as mould for the composition of new additional chain. Thus
the two affiliated molecules that result are facsimiled with the corpus and
each one is constituted by an old and a new chain. The mechanism it was named semi
conservative.The maternal molecule of DNA is constituted by two additional chains
of DNA. Every base is connected with bond of hydrogen with additional A with T
and G with C. Initially they separate two chains of DNA and each maternal chain
functions as mould for her creation new maternal chain.Nucleotides are connected
between them with fosfodiesteric bonds in order to create the two new chains. Each
affiliated molecule is constituted by a maternal and a new chain. Because of this the
mechanism of copy is named semi conservative copy of DNA begins from
determined points that are named places beginning of copy. The copy begins as
already it has been reported from places of beginning of copy. Special proteins that
are in charge of beginning of process of copy they are attached in regions with
concrete concatenation of bases in the DNA and cause the unfolding of two
chains creating with this way one open "bight" in the DNA that is visible even with
optical microscope. To this direction help also the DNA elicases special ferments that
break the bonds hydrogen in order to becomes the unfolding of chains. In the DNA
chromosomes of eukaryotic cells they are observed many bight's indicative his that
the copy becomes simultaneously from a lot of places beginning. Finally bight's they
are linked between them and with this way are gained precious time and the copy of
DNA are fulfilled in few only hours.
As soon as it is created bight the copy begins and is continued to the two directions,
always with direction 5 ' to 3 ' the new chain up to the completion of copy of entire
molecule of DNA. In two utmost bight's it is observed a crotch copy that it represents
the points of elongation of new chains of DNA.
Special ferments that are named DNA polymerases are responsible for elongation of
new chains of DNA. As nucleotides are aligned with additional nucleotides in the
"old" chain DNA polymerases they connect between them in utmost the new chain
that it is elongated. The rhythm of elongation reaches the 500 nucleotides at
second in the bacteria and the 50 at second in human cells. The DNA polymerases do
not have the possibility of beginning copy. What they can make is add nucleotides in
poly nucleotides chain that already exists. This chain that is constituted from 10
roughly nucleotides is named fundamental department and in reality is a small in size
chain RNA. A ferment that is named primasi connects nucleotides RNA and with this
way is created fundamental department RNA. The DNA polymerases undertake in
continuity action and they connect nucleotides DNA in the fundamental department
creating and elongating of a new chain DNA. New molecules DNA are created as
take shape bonds of hydrogen between additional nitrogenous bases of two chains old
and new. The DNA polymerases they can still correct also errors that happen at the
duration polymerases are repaired to a large extent from specifically repairing
ferments.
Expiry: The elongation stops in codon of expiry (UGA UAG or UAA) because they
do not exist tRNA that would correspond in them. code of expiry it is recognized by
the factor of release which causes the expiry and the release of polypeptide chain as
well as splicing of two subunits of ribosome. Immediately hardly the ribosome has it
translates the first code the place of mRNA is free for mooring of other ribosome. The
cluster of ribosomes that it is created with mRNA it is named polysoma. The
regulation of expression of genes in the eukaryotic cells becomes with
particularly complicated mechanisms and it is the subject of intensive
research. The complete clarification of this mechanisms perhaps gives answers
for how and when this mechanisms disordinate the cells how"they come out" from
the strict program of their operation and become cancer cells. In the eukaryotic cells
the gene expression is regulated in four levels: a)in the level of transcription b)in level
afterwards the transcription (mechanisms of maturation of precursor mRNA) c) in the
level of translation (time survival of molecules mRNA in the cytoplasm) and in level
afterwards translation (modification of protein in order to is rendered active).
We will try therefore for afterwards of the examination that we made with regard to
the doubling and the mitosis to prove in whitch way an all physiological DNA with
the production of a physiological mRNA it produces defective proteins at their
translation. whitch they are not recognized by the cell at the later modification so to
renders them active and they can act as molecular switch transporting the proportional
information in the cell on his physiologic operation.Thus the cells disordinate and
come out from the strict program of their operation and they become cancer cells.
And how this is happens we will see it now immediately.Each tRNA it is connected
with corresponding amino-acid after it is activated first from proportional aminoacyl-
tRNA synthetases who is a ferment expert for each amino-acid. The first codon of
mRNA is always AUG and in what attached tRNA brings amino-acid methionini
However do not have all the proteins of organism as first amino-acid methionini. This
happens because in a lot of proteins afterwards their composition are removed their
certain amino-acids from aminic utmost. The composit whitch is created afterwards
the mooring of mRNA in his small subunit ribosome and tRNA that transports
methionini it is named composit beginning the proteinosyntesis. and the big subunit
is then connected with small. At the elongation a second molecule of tRNA with
anticodon additional to the second codon of mRNA it is placed in suitable admission
of ribosome transporting the second amino-acid. Between methionini and the second
amino-acid takes shape a peptide bond and immediately afterwards the first tRNA
disconnect by ribosome and is released in the cytoplasma where it is connected again
with methionini ready again for next use. The ribosome and mRNA they have now
tRNA above in that it is attached two amino-acids. Thus begins the elongation of
polypeptide chain. Then the ribosome it moves at length mRNA at code A .a third
tRNA comes attached transporting his amino-acid . between the second and the third
amino-acid takes shape a peptide bond. The polypeptide chain continues to be
elongated as a new tRNA bring amino-acids which connect between them.For shaping
of peptide bond and the detachment tRNA from ribosome needs the catalytic action of
a ferment.Each tRNA-aminoacid is katalysed by a different ferment. The Absence of
some ferments of disactivation tRNA-aminoacid it has as a result the welding of
molecule tRNA in the final product of protein. We have therefore a protein with
adjacent connection of molecule tRNA with a result when it is completed and at the
later modification so when the protein it is rendered active to be not recognized by
the cell. Therefore we have wrong protein accordingl wrong information to the cell to
pause the beginning of operation with result the complete disordination of cell and
incoherent and his unverifiable course for his cancer situation. Very probably
cell it does not receive the information of finising mitosis process so that it continues
dividing making each time errors.
Amino-acids. the shaping of peptide bond between the –NH3 of an amino-acid and a-
COOH of an other it is thermodynamic unfeasable. This obstacle is passed activating
his -COOH the precursors of amino-acids. The activated intermediary molecules in
composition of proteins is esters of amino-acids in that -COOH an amino-acid is
connected or in the 2 ' - or in the 3'-of riboze of the nucleotide 3 ' utmost tRNA. This
activating intermediary molecule is called amjnoakylo-tRNA.The mooring of amino-
acid in tRNA is important not only because it activates the - COOH but also because
the amino-acids cannot recognize alone the codon of mRNA. The amino-acids it
should be specifically transported in the ribosomes from tRNA that can recognize
codons mRNA and acting as adoptive molecules.The first step of activation of amino-
acids is the shaping aminoakylo-adenyl from a amino-acid and a molecule ATP Takes
shape a intermediary molecule (mixed anhydride) in which - COOH of amino-acid is
connected with the fosforic team of AMP. For this reason this intermediary molecule
is known and as aminoakylo-AMP.
The next step is the transport of aminoakylo-AMP in a molecule tRNA and the
shaping amjnoakylo-tRNA that is the activated intermediary molecule in the
composition of proteins. In certain molecules tRNA the amino-acid is transported in
the 2'-OH of roboze while in other in the 3'-OH.The sum of reactions is a total
reaction exceptionally outenergy: Aminoacid + ATP + tRNA + H2O aminoakylo-
tRNA + AMP + 2Pi Consequently two fosforic bonds of high energy are consumed
for the composition aminoakylo-tRNA. The one of them is consumed for shaping of
esteric connection aminoakylo-tRNA while the other it is front used for the impulse of
reaction to the activation of amino-acids and their consequent connection with tRNA
katalysed from special synthetases aminoakylo-tRNA whitc also are called activated
ferments. aminoakylo-tRNA synthetases are exceptionally selective ferments as for
his recognition so much amino-acid that is to be activated as the receptor tRNA.The
street that follows the tRNA via medium ribosome for production of polypeptide
(protein) is A place-P place-E place. place E is the one which is the place of expense
tRNA that was previously in place P.
The absence of therefore ferments of activation and disactivation which are special
ferments for each amino-acid peptidyl-tRNA aminoacyl-tRNA it leads to the eve of
more tRNA to the final product protein so that it renders the protein defective.
That is to say in conlusion in the final product of protein instead to contain only the
essential amino-acids which is identifid it contains also in some point “certain
points” of protein and the tRNA in the final product of protein.resulting the final
product of protein of being defective and not transports the same message in the cell
so it is disordinate all mitotic process.
The digestion of proteins Already has been reported the action [pepsins] in the
stomach. The smaller [polypeptides] (products of action [pepsins]) they are changed
in amino-acids or in smaller chains the two or three amino-acids. Thrypsine and
chymothrypsine ([pagkreatik] proteolytical ferments) they split big [polypeptides]
chains in smaller chains. The [carboxypeptidase’s] breaks away amino-acids from
utmost the chain with [karboxylomada]. The [aminopeptidase’s] breaks away amino-
acids from utmost with [aminomada]. [Dipeptidases] the thin intestine they split small
[peptidikes] chains in amino-acids.
Three by the ferments that [ekkrinei] the pancreas, that is to say, [thrypsini], the
[chymothrypsini] and [carboxypeptidase’s], [ekkrinontai] in inactive form and they
are activated only in the presence [enterokinase (is said also enteropeptidase), ferment
of thin intestine.
Telomerase
a ferment that it substitutes the [telomeres] naturally utmost
chromosomes
Promotes the regenerative faculty of cells
They are constituted from repeated not genetic material and they are covered by
proteins
the unverifiable differentiation of cells that leads to the cancer is owed in the absence
of proteins that covers the telomerase and renders him inactive in the physiologic
cells.
lets see therefore why shaping proteins
1. Does not exist the gene expression
for the biosynthesis of 10 essential amino-acids.
2. Because lack of ferments of digestion
([thrypsine] [chymothrypsine] etc)
3. because lack enterokinase.
Because therefore lack of gene expression in the
human genome of required ferments for the biosynthesis of 10 essential amino-acids
the organism should receive him from the foods
afterwards [katabolism] the proteins from the ferments of digestion. ([thrypsine]
[chymothrypsine], etc)
Was examined the creature of 5 patients with cancer with the method of quantitative
analysis of free amino-acids and were found decreased prices of amino-acids and
the most lysine then we will detect the level of trypsine and [enterokinase] for
which We believe that or the [enterokinase] does not activate trypsine or trypsine
disengaged from a1-[antitrypsine] or exists insufficient engagement lysine from the
organism.
The research is continued for further investigation.
Ferments to investigation.
tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (tRNA(m7G46)-
methyltransferasetRNA isopentenyltransferase, mitochondrial precursor
(EC 2.5.1.8)
(Isopentenyl-diphosphate:tRNA
isopentenyltransferaseglutamyl-tRNA(Gln) amidotransferase subunit B,
mitochondrial precursor (EC 6.3.5.- adenosine deaminase,tRNA-specific
tRNA-nucleotidyltransferase 1, mitochondrial precursor (EC 2.7.7.25)
(Mitochondrial tRNA
nucleotidyl transferase, CCA-adding) (mt tRNA adenylyltransferase)
(mt tRNA CCA-pyrophosphorylase) (mt tRNA CCA- diphosphorylase) (mt
CCA-adding enzyme).
Arginyl-tRNA--protein transferase 1
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
Methionyl-tRNA formyltransferase, mitochondrial precursor
N(2),N(2)-dimethylguanosine tRNA methyltransferase
UGA suppressor tRNA-associated protein (tRNA(Ser)Sec-associated
antigenic protein) (
tRNA pseudouridine synthase 3 (EC 5.4.99.-) (tRNA-uridine isomerase
3)(tRNA pseudouridylate synthase
N2,N2-dimethylguanosine tRNA methyltransferase-like
tRNA-(N1G37) methyltransferase
Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine
transglycosylase) (Guanine insertion enzyme).
glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1
Peptidyl-tRNA hydrolase 2, mitochondrial precursor
tRNA phosphotransferase
queuine tRNA-ribosyltransferase domain containing 1 [
tRNA-splicing endonuclease subunit Sen2 (EC 3.1.27.9) (tRNA-intron
endonuclease Sen2)
tRNA splicing endonuclease 34 homolog
L-seryl-tRNA(Ser/Sec) kinase (EC 2.7.1.-) (Phosphoseryl-tRNA(Ser/Sec)
kinase).
tRNA-splicing endonuclease subunit Sen54 (tRNA-intron endonuclease
Sen54)
Exportin-T (tRNA exportin) (Exportin(tRNA)).
tRNA glutamine 1
tRNA-splicing endonuclease subunit Sen15
tRNA isopentenyltransferase 1
tRNA nucleotidyl transferase, CCA-adding, 1 (TRNT1) pseudogene
adenosine deaminase, tRNA-specific 1
Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (Ribonuclease Z
2)
Zinc phosphodiesterase ELAC protein 1 (EC 3.1.26.11) (Ribonuclease Z
1
Selenocysteine-specific elongation factor
Glutaminyl-peptide cyclotransferase precursor (EC 2.3.2.5) (QC)
(Glutaminyl-tRNA cyclotransferase) (Glutaminyl cyclase).
Peptidyl-tRNA hydrolase 2, mitochondrial precursor (EC 3.1.1.29) (PTH
2)(Bcl-2 inhibitor of transcription 1).
Acetyl-CoA acetyltransferase,
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthethase 1
(PAPS synthethase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK1) (SK 1)
[Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (Sulfate
adenylate
transferase) (SAT) (ATP-sulfurylase); Adenylyl-sulfa
23S rRNA methyltransferase/RumA
23S rRNA methylase leader peptide
23S rRNA (uracil-5-)-methyltransferase RumB
rRNA methyltransferase 3 (EC 2.1.1.-) (rRNA (uridine-2'-O-)-
methyltransferase 3).
rRNA processing protein EBP2 (EBNA1 binding protein 2) (Nucleolar
protein p40).
SSU_rRNA_5
5S_rRNA,
RNA methyltransferase 2 (EC 2.1.1.-) (rRNA
(uridine-2'-O-)-methyltransferase
dimethyladenosine transferase (EC 2.1.1.-) (S-
adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase) (18S
rRNA dimethylase).
ribosomal RNA methyltransferase 1 (EC 2.1.1.-) (rRNA
(uridine-2'-O-)-methyltransferase)
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