PROTEINS: STRUCTURE

AND FUNCTIONS

Claudia Hernández Troncoso

Medicine student

III semester

Faculty of medicine

School of health sciences

Universidad Pontificia Bolivariana

o

FOLDING

FOLDING 2

INTRODUCTION

macromolecules

formed by amino

acid chains joined for

peptides links they

have a big cellular

activity

each protein is a only

codified sequence

which can changes

as the different

structure levels, the

principal actions

inside and outside

cell

NEWS #1

Now the project is expanding into the HUPO, the Human

Proteome Organization

a number of proteins associated with

prostate cancer are controlled by

chromosome 19

MAPPING PROTEINS ON CHROMOSOME

19

HUPO

There are over 20 000

proteins coded by the

genome in the human body

Each protein has an unique

encoded structure

all functions depends of

variability sequence of

amino acid and the

different levels of

structures

CROMOSOME 19

MAPPING PROTEINS ON CHROMOSOME

19

CROMOSOME 19

SUPPORT 63 MILLONES

PARS OF BASES

CONTAINS BETWEEN 1,300 AND 1,700

GENS

IT HAS THE PSA: PROSTATE

SPECIFIC ANTIGEN

RELATIONSHIP BETWEEN THE PROTEINS AND

PROSTATE CANCER

PROSTATE CANCER• Is an adenocarcinoma more common in the peripheral zone

• may cause:

pain

Difficulty in urinating,

Problems during sexual intercourse,

Erectile dysfunction

• PSA is a tumor markers to determine the

origin of malignant cells that have metastasized

MAPPING PROTEINS ON CHROMOSOME

19

MAPPING PROTEINS ON CHROMOSOME

19

Medicine for the current is critical analysis

of the components of the human genome

and the evolution through the same, which

may generate some type of disease, therefor

e believe that the

proteins is a structural model of analysis and

set up to oriented to XXI century needs to

develop technologies that can fight

cancers, besides the use of new drugs.

NEWS # 2

Interactions between

proteins are of

fundamental

importance for a

number of processes in

virtually every living cell

In the process of protein folding one of the

partner don’t have the active configuration but it was purchased at the

union time

MYSTERY ABOUT RECOGNITION OF UNFOLDED

PROTEINS SOLVED: THE LOCK SHAPES THE KEY

FOLDING

the process by which a protein reaches its structur

e tridimension

The biological function of a protein depends on

its correct folding.

unions between protein-protein are due

to the hydrogen bonds and van der waals forces

to form the basis of three-dimensional structures

beta sheets and alpha helices

STRUCTURE LEVELS

MYSTERY ABOUT RECOGNITION OF UNFOLDED

PROTEINS SOLVED: THE LOCK SHAPES THE KEY

Primarystructure

• Lineal position of amino acid

• Covalents links between aminoacids

Secundarystructure

• Structure tridimentional form

• beta sheets and alpha helices

tertiarystructure

• Folding between beta sheets and alpha helices

• Interactions no covalent links as hydrogen bonds and van der waals force

quaternary structure

• Union between many peptide chains

• Globular forms

ENZYME RIBONUCLEASE S

in its active form comprises

the S-protein and an α-helical

S-peptide

S-protein has a defined three-dimensional shape, the S-peptide on its own is initially

unfolded

the S-protein recognizes the unstructured S-

peptide or a small fraction of peptide molecules in their

helical conformation

Protein-protein recognition in this case takes place via hydrophobic

interaction of the S-protein with two

spatially clearly defined areas of the unstructured

S-peptide.

MYSTERY ABOUT RECOGNITION OF UNFOLDED

PROTEINS SOLVED: THE LOCK SHAPES THE KEY

MYSTERY ABOUT RECOGNITION OF UNFOLDED

PROTEINS SOLVED: THE LOCK SHAPES THE KEY

Knowledge of the structural

configurations of proteins is essential for the

analysis of the respective cellular functions

and thus be able not only to understand its

complexity if not interact with

them to reach between protein folding thus pr

ovide an opportunity for science to modulate

their

activities and functions thus leading to greate

r scientific breakthrough.

MEDICAL UTILITY

MEDICAL UTILITY

A single amino acid, wrong folding, and wrong hydrogen bonds-may cause a clinical issue with disastrous consequences for the patient

Studies about them are important not only because their damage implications in clinical areas

MEDICAL UTILITY

Proteins areimportant for thedevelopment andresearch of newmedicaments andtherapies

MEDICAL UTILITY

BIBLIOGRAPHY

• MARTINEZ SÁNCHEZ, Lina María. Biología molecular. 2. ed. Medellín: UPB. Fac. de Medicina, 2006. 105 p.

• COOPER,GM.. La célula. 2ed. Madrid :Marban, 2002. 76-79 p

• LODISH, h. Biología celular y molecular. 5ª edición. Buenos Aires: Medica Panamericana, 2004. 355 p

• “mapping protein in the chromosome 19” onsciencedaily.com

• “mystery about recofnition of unfoulded pro teinssolved: the lock shapes the key” onsciencedaily,com

THANKS YOU!!