Exam 3 Flashcards
Structure of Proteins and function
Connective tissue- collagen
muscle
Function of proteins
muscle contraction
enzymes
some hormones
Enzymes
all enzymes are proteins
Hormones
-insulin
-growth hormone
-glucagon
-epinephrin, norepinephrin
derived from a single amino acid
how many amino acids
20
R
is a side chain
amino acids combine to form proteins by
amide proteins
primary structure
amino acid sequence
secondary structure
arrangement of amino acids in “space”
tertiary structure
three dimensional shape
caused by folding, coiling, sheeting
quaternary structure
protein subunits combined to form 1 protein
how are amino acids classified
based on the structure of the side chain
order or sequence of amino acids
determine how the amino acids will interact with each other
how does the sequence influence long chains
influences the bend and fold as a protein develops
the final 3D shape is determined
sequence of amino acids
Bioactive proteins
resistance relies on a series of events that triggers the enzymes
Bioactive protein examples
hormones like insulin, growth hormone, glucagon
genetic code for insulin
transcribed into a nucleotide sequence complementary to the DNA strand
complimentary strand of nucleic acids in DNA message
messenger RNA
mRNA interacts w/
ribosomes so that the message is translated
set of 3 consecutive nucleic acids
codon
codon
specific for a particular amino acid
What reaction results in the formation of a peptide bond
In proteins or peptides, amide bond formed by reaction of amino group of one amino acid and the carboxylic acid
simplest amino acid
glycine (only side chain consisting of only hydrogen)
Non-polar side chains
alkane side chains (CH)
Ala
Val
Leu
Ile
Non-polar side chain
has -NH group bound to 2 C
Imino group
Proline
- amino group and aromatic group
- aromatic to a single methyl
- sulfur bound to two carbons
Trp
Phe
Met
polar side chains with a pH 7.0 electrically neutral
-polar group (OH)
(SH)
Ser
Thr
Cys
Tyr
polar acid side chain ionized with pH 7.0 negative charge
-caboxylic acid
(acidic amino acids)
Glu
Asp
amino group attached to carboxyl-carbon
Gln
Asn
polar pH 7.0 positive charge (polar basic side chains)
His
Lys
Arg
How is the genetic code read and converted into the sequence of amino acids in a protein
genetic code –> double helix 1 strand per half consists of nucleotides–> read and transcribed by RNA developed by enzymes
Biotin
Biotin
CO2 fixation
Pantothenic acid
Coenzyme A
Acyl group transfer
Riboflavin (B2)
Flavins (FAD)
oxidation-reduction
Niacin
Nicotinamide (NAD)
oxidation-reduction
Pyridoxine (B6)
Pyridoxal phosphate
transamination
Thiamine
Thiamine pyrophosphate
aldehyde transfer
Essential amino acids
any amino acid that cannot be made
Non-essential amino acid
amino acids that can be synthesized by the animal and do not need to be in the diet
Indispensable amino acid
ruminant- ruminal microbes convert dietary proteins to microbial proteins, which contain essential amino acids
kinase
enzyme that catalyzes transfer of a phosphate from ATP
Enzyme hydrolase catalyzes
hydrolysis
oxireductase
oxidation and reduction