17.11.

2011

Repasemos
la formacin
Protenas de una
protena
Prof. Wilkesman

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Amino Acid Sequences Have Direction Proteins

This illustration of are linear polymers built of monomer units
the pentapeptide
Tyr-Gly-Gly-Phe- called amino acids.
Leu (YGGFL)
shows the contain a wide range of functional groups.
sequence from the can interact with one another and with
amino terminus to
the carboxyl other biological macromolecules to form
terminus complex assemblies.
Some are quite rigid, whereas others
display limited flexibility
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MW de protenas Podemos clasificarlas?

MW en g/mol Fibrosas
Forma filamentosa
MW en Da
Funcin estructural en clulas y tejidos
MW promedio de los aa= 110 Ej.: protenas de la piel, tejido conjuntivo, fibras
N aa encontrados en prot.= 50-2000 animales
Globulares
MW prom de las protenas=?
Forma de globo por plegado de la cadena
polipeptdica
Funciones: trabajo qumico de la clula
Ej.: Mioglobina, hemoglobina,
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Estructuras de organizacin en
Ej: Insulina
protenas
Amino Acid Sequence of Bovine Insulin. Estructuras:
1 -> secuencia de aa
2 -> hlices , lminas
3 -> plegado de la estruct. 2
4 -> Empaquetado de estructuras 3

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Lminas beta

Hlices alfa

Structure of a Strand. The side chains (green) are alternately above and below
the plane of the strand

Structure of the Helix. (A) A ribbon depiction with the -carbon atoms and side chains (green) shown. (B) A
side view of a ball-and-stick version depicts the hydrogen bonds (dashed lines) between NH and CO groups. (C)
An end view shows the coiled backbone as the inside of the helix and the side chains (green) projecting outward.
(D) A space-filling view of part C shows the tightly packed interior core of the helix.
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Lminas
Lminas beta mixtas
beta
An Antiparallel
Sheet. Adjacent
strands run in opposite
directions. Hydrogen
bonds between NH and
CO groups connect
each amino acid to a
single amino acid on an
adjacent strand,
stabilizing the structure.

A Parallel Sheet.
Adjacent strands run
in the same direction.
Hydrogen bonds
connect each amino
acid on one strand with
two different amino Structure of a Mixed Sheet
acids on the adjacent
strand.
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Dihedral angles
A measure of the rotation about a bond, usually between
-180 and +180. Sometimes called torsion angles
Rotation About Bonds in a
Polypeptide. The structure of each
amino acid in a polypeptide can be
ngulos de
adjusted by rotation about two
single bonds. (A) Phi () is the
angle of rotation about the bond
rotacin
between the nitrogen and the -
carbon atoms, whereas psi (y) is
the angle of rotation about the bond
between the -carbon and the
carbonyl carbon atoms. (B) A view
down the bond between the
The structure of each amino acid in a polypeptide can be adjusted by rotation about two single nitrogen and the -carbon atoms,
bonds. (A) Phi ( ) is the angle of rotation about the bond between the nitrogen and the -carbon showing how is measured. (C) A
view down the bond between the -
atoms, whereas psi () is the angle of rotation about the bond between the -carbon and the carbon and the carbonyl carbon
carbonyl carbon atoms. (B) A view down the bond between the nitrogen and the -carbon atoms, showing how y is
atoms, showing how is measured. (C) A view down the bond between the -carbon and the measured.
carbonyl carbon atoms, showing how is measured.
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Representaciones de
Ramachandran
Convenio
Ilustracin que representa las
conformaciones permitidas. Pueden existir
muchas combinaciones de estructuras
secundarias, pero slo algunas son
factibles. Las coordenadas son los
ngulos psi () y phi ()

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Ramachandran
Ramachandran
Diagram for
Helices
Both right- and
left-handed helices
lie in regions of
allowed
conformations in
the Ramachandran
diagram. However,
essentially all
helices in proteins
A Ramachandran Diagram Showing the Values of and psi. Not all and psi
are right-handed.
values are possible without collisions between atoms. The most favorable regions are
shown in dark green; borderline regions are shown in light green. The structure on
the right is disfavored because of steric clashes.
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Ramachandran Diagram For Strands

The red area

shows the
sterically
allowed
conformations of
extended, -
strand-like
structures

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Ejemplos de protenas fibrosas Alfa - Queratinas

Queratinas
Colgeno

An -Helical Coiled Coil. The two helices wind

around one another to form a superhelix. Such
structures are found in many proteins including
keratin in hair, quills, claws, and horns.
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Colgeno
The structure of a typical collagen
molecule.
(A) A model of part of a single collagen
chain in which each amino acid is
represented by a sphere. The chain is
about 1000 amino acids long. It is
arranged as a left-handed helix, with
three amino acids per turn and with
glycine as every third amino acid.
Therefore, an chain is composed of
a series of triplet Gly-X-Y sequences,
in which X and Y can be any amino
acid (although X is commonly proline
and Y is commonly hydroxyproline).
(B) A model of part of a collagen
molecule in which three chains, each
shown in a different color, are wrapped
around one another to form a triple-
stranded helical rod. Glycine is the
only amino acid small enough to
occupy the crowded interior of the
triple helix. Only a short length of the
molecule is shown; the entire molecule
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Protenas 2

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Protenas globulares: estructura

Modelos de plegado
terciaria, modelos de plegado
La mayora de las protenas estn formadas por ms de un
dominio
Existen ciertos motivos comunes en
Existe siempre un interior de residuos hidrofbicos y un protenas:
exterior de residuos hidroflicos. Todas tienen ms de un dominio
Las lminas estn generalmente envueltas en
estructuras cilndricas.
Hay un interior hidrofbico y un exterior
Existen giros en la cadena polipeptdica para doblar en
hidroflico
esquinas o ir de un segmento a uno o viceversa. Tipos Lminas beta estn envueltas en estructuras
de giros: y . tipo cilindro
No todas las partes de las protenas globulares son hlices
o lminas , o giros. Existen segmentos conectores o Hay giros
regiones estructuradas irregularmente. No todo es hlices alfa, o lm. Beta, tambin
hay segmentos conectores
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Tipos de
Dominios de protenas Giros:
Protein Domains. The cell-surface protein CD4
consists of four similar domains
Dominio: regin compacta, plegada localmente,
de la estructura 3

Giro tipo
Giro tipo
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Tipos de plegados de
Barriles beta protenas globulares

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Ejemplo de
protena rica Qu est sucediendo?
en lminas
beta
Immunoglobu
lin Fold. An
immunoglobuli
n domain
consists of a
pair of -
sheets linked
by a disulfide
bond and
hydrophobic
interactions.
Three
hypervariable
loops lie at one
end of the
structure.
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Estructura Nativa Desnaturalizacin

Renaturalizacin Estabilizacin de la estructura 3
Factores que
determinan las
a) Interacciones carga-carga
estructuras 2 y 3. b) Puentes de hidrgeno internos. Hay tres
Desnaturalizacin y tipos: armazn con armazn, armazn con
agentes
desnaturalizantes. cadena lateral y cadena lateral con cadena
Papel del S-S. lateral.
La mayora de la c) Fuerzas Van der Waals
informacin que d) Efecto hidrofobo: el enterramineto de los
determina la
estructura 3-D de grupos R hidrofobos en el interior de la
una protena la protena produce un aumento de la entropa
lleva la secuencia de estabilizacin.
de aminocidos.
e) Puentes S-S: formados exclusivamente
por Cys
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Estabilizacin por puentes de H

Estructura cuaternaria
Asociacin de cadenas
polipeptdicas para formar
estructuras especficas de
mltiples subunidades.
Qu estabiliza la estructura
4?
Las mismas interacciones que
estabilizan la estruct. 3.

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Hemoglobina

Mioglobina
Three-Dimensional Structure of Myoglobin. (A) This ball-and-stick model
shows all nonhydrogen atoms and reveals many interactions between the
amino acids. (B) A schematic view shows that the protein consists largely of
a helices. The heme group is shown in black and the iron atom is shown as
a purple sphere.
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Importancia Importancia
biolgica de la biolgica de la
hemoglobina hemoglobina

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