Aminoacids and

Proteins
Bioqumica
Guarina Molina

20 aminoacids found
in proteins

amino group attached

to alpha-carbon +
side chain +
hydrogen atoms

Classified according to their side

chains: polarity (charged, nonpolar
hydrophobic or uncharged polar) and
structure (aliphatic, cyclic or aromatic)

Nonpolar aliphatic

Within proteins they cluster together

to form hydrophobic cores (att.
valine in sickle cell anemia)

electrons are shared equally so their

hydrogen cant bond with water

glicine has a small chain and it is

used to tighten up fibrous proteins
(att. collagen)

Aromatic Aminoacids

Contain a ring with

same structure but
their polarities are
very different

PHE - very nonpolar

hydrophobic

TYR - its OH group

causes it to form
hydrogen bonds and
its more hydrophilic

TRP - more polar than

PHE due to its indole
ring

Aliphatic, Polar, Uncharged Aminoacids

Contain an amide or
hydroxyl group

Asparagine and
glutamine are amides
of AA aspartate and
glutamate

Hydroxyl groups help

form bonds with
water

Commonly found in
the surface of
water-soluble
globular protein

Sulfur-containing amino acids

Protein albumin has disulfur bond

Basic: side
chains have
nitrogen;
they accept
protons and
have positive
charge

Acidic and
basic AA
participate in
hydrogen
bonding to
form salt
bridges

Acidic and basic amino acids

These 20 AA derive other amino acids through different

processes that add groups to the AA ex. hydroxyproline
and hydroxylisine derive from proline and lisine through
hidroxylation with the enzymes x-hydroxylase

Aminoacid derivatives

Proteins

Classification of proteins

Classification according to their biological structure

Primary Structure

p. 103 Marks

Variations of primary structure

p 78 (Marks)

Polymorphism in protein structure (alleles, point

mutations)

Proteins families and superfamilies

Developmental variation (HbF changes to HbA after

birth)

Tissue-specific isoforms (CK-MM/MB/BB)

Some species variations in the primary structure of

insulin (p. 81)

Protein Families

Have related
functions and
similar
structures

Similar but
not identical
structures

Evolved from
the same
gene
(sometimes)

Secondary Structure

Polypeptide chains form

recurrding, localized structures,
organized in alpha-helix and
beta-sheets.

Difference: in the
alpha-helix the peptide
backbone hidrogen
bond are in the same
strand, but the betasheets have it parallel
to each other.

Tertiary Structure/Quaternary Structure

Tertiary structure:
folding pattern of
the secondary
elements into 3D
conformations.
Flexible and
dynamic.
Use hydrogen
bonds, ionic
bonds, van der
Walls interactions
and disulfide bond
formation to stay
together.

Quaternary structure:
A protein that has several subunits that combine to make 1
functional protein. Example: hemoglobin that consists of 4
chains

Protein domains

Distinct functional/structural
units in a protein that makes
the protein have interactions

Every domain has 40 - 400

amino acids

Marks:
Domains can be identified by visual
examination of a 3D figure of the
protein. Each domain is formed by a
continous sequence of amino acids in
the polypeptide chain.

Protein folds (plegamientos)

Large patterns that are recognized in proteins of

different origins related to a specific activity.

Ex.

actin fold: found in actin, hexokinase and

heat shock protein. Have the same large
conformational change that gives the protein
a specific fnction (bind ATP)

Protein denaturation
p. 105

Denaturation through non-enzimatic

modification of protein: glucolysation or
oxidation

Protein denaturation by temperature, pH and

solvent

Protein misfolding/Prions