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The building block of proteins are
amino acids
3 types of proteins
simple
conjugated
derived
Simple proteins yield what products when broken down?
amino acids or products of amino acids
conjugated proteins yield what products when broken down?
amino acids and non-protein compounds
hemoglobin, myoglobin and immunoglobins are examples of
conjugated proteins
The globin (protein) of hemoglobin is complex to a
non protein heme
immunoglobulin is complexed to
a carbohydrate
Derived proteins
made in an inactive state and become activated as a result of some chemical triggering device. TYpically have the prefix pro- or the suffix -ogen
An amino acid contains
an amino group (NH
2
) and a carboxyl (-COOH) group linked by a carbon atom called the alpha carbon.
Amino acid deionizes to form
H+ and conjugate base
Essential Amino Acids
Arginine
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
Non-essential amino acids
glycine
serine
cysteine
alanine
glutamic acid
aspartic acid
asparagine
glutamine
proline
tryosine
The most important aspect of the structures of an amino acid from a chemical standpoint is
the R Group
Amino acids are amphoteric meaning
they react with acids and/or bases
If an amnio acid is acidic then
it hase two or more carboxyl groups and one amine group and a has a negative charge
If an amino acid is basic
it contains two amino groups and one carboxyl group and has a net positive charge.
The pH at which the carboxyl group is 1/2 ionized or at equilibrium is the
pK
The isoelectric point (pKa) is
the pH at which the amino acid is one-half ionized and is neutral
the bond between the fatty acid and alcohol is called
ester bond
a peptide bond forms between
amino acids
A glycoside bond is formed between
glycogen (sugars)
The primary structure of a protein is:
the amino acid sequence that determines the
configuration
of the amino acid
the secondary structure of a protein
determines the
conformation
or relationship of amino acids in procimity to each other within the sequence. called
first folding
.
eg
: alpha helix or beta pleated sheet
Tertiary structure of protein
second folding.
the interaction of distanct amino acids at various locations within the sequence
Quartenary structure
the complexing of at least two tertiary proteins. there are four tertiary proteins to a quartenary protein held together by covalent bonds.
oxyglobin is ___ protein and deoxyglobin is ___ protein in lungs
relaxed; flexed
Function of proteins
Support
movement
transport
buffering
metabolic regulation (thru enzymes)
coordination and control (protein hormones)
defense (waterproof proteins of skin, antibodies and clotting proteins)
Two types of proteins
fibrous
globular
Role of fibrous proteins
generally structural
role of globular proteins
often make up enzymes, hormones and molecules that circulate in bloodstream
3 basic characteristics of enzymes
specificity
saturation limits
regulation (using cofactors to activate of deactivate enzymes)
Collagen appears in
Type 1
: skin, tendon, bone and cornea of eye
Type 2
: menisci and intervertebral disks
Type 3
: fetal cardiovascular tissue
Type 4
: basment membrane.
Globular protiens have what typoe of conformations?
tertiary and quartenary
Enzymes are comprised of a protein portion called
apoenzyme and a non-protein portion co-enzyme
Enzymes are
biological catalyst
Enzymes are affected by
pH and temperature
coenzymes are derived from ___ and must bond to ___ before substrate binding can occur
vitamins; enzyme
Difference between RNA and DNA
RNA is a single strand and DNA double Helix
RNA has Uracil and DNA has Thymine
Three types of RNA
messenger
transfer
ribosomal
Nucleic acids: function and composition
store and process information at the molecular level
made of purines and pyrimadines
Nucleic acids are chains of
nucleotides
nucleotides are composed of
a sugar
a phosphate
nitrogenous base
Author
hoyadavis
ID
22814
Card Set
Proteins
Description
function of protien in body
Updated
2010-06-09T17:33:10Z
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