Proteins Flashcards
(27 cards)
Basic unit of proteins made of
Amino acid
Elements in all parts of amino acid
Nitrogen, Oxygen, Hydrogen and Carbon
Structure
top side varies, nitrogen combined to two hydrogen, carbon to hydrogen, carbon off of carbo to oxygen to hydrogen, carbon to oxygen C-O-H is acid group
H-N-H is amino
How many
20 amino acids
Essential
This is needed from dietary forms as we cannot make this is our bodies
Indispensable
cannot be synthesized by the body
Step 1 of Synthesis
Cell signally- the cell signals the body to create protein, this happens in the cell membrane. it moves inside of the cytoplasm of a cell. it regulates what the body needs
Step 2- Transcription
This transcripts the amino acid to form the sequence of protein. it happens in the nucleus. mRNA uses DNA to make this. mRNA binds to the gene to form mRNA strand and moves to the cytoplasm. carries the info needed
Step 3- Translation
linkes together from the peptide bonds on ribosomes using mRNA and tRNA. Ribosome can build up the proteins. The ribs joins connects the polypeptides via peptide bonds.
Gene
protein of chromosome codes for primary structure of a protein
Chromones
Strands of DNA, packed with the proteins in a nucleus and has 23 pairs
DNA
Codes for synthesis of a protein, nucleus
Name of reaction that joins amino acid
Protein synthesis
Primary structure of proteins
The first level of protein structure; the specific sequence of amino acids making up a polypeptide chain
sequence in amino acids, polypeptide chain held together by covalent bonds. made by translation.
Secondary Structure
coiling or folding, a- helix, B- folded sheets. weak bond causes alpha helix
-Hydrogen bonds between a repeating polypeptide backbone
Quaternary
2 or more peptide chains come together polypeptide chains come tougher to form final protein
Protein Digestion: stomach
pepsin is active enzyme in stomach which breaks bond to hold muscle together
1) releases HCl
2) HCL activity pepsinogen (inactive)
3) Pepsin breaks down protein/ peptides
Small Intestine
The pancreatic and small intestinal proteases breaks down the polypeptides and creates dipeptides, tripeptides and amino acid
Denaturation
is the destruction of proteins that alter or unfold to a 3D form,
Cause of denaturation
a loss of biological activity
it loses quaternary structure, territory structure and secondary structure present in their native state by application of some external stress of compound such as a strong acid or base
caused by external stress
Absorption of amino acids
are taken up by dipep and tripeptdes taken up by enterocytes. more digestion for amino acids
Transport: amino acids in blood- portal route,
Metabolize amino acids
comes from diet and endogenous 1- protein synthesis from dietary and engines sources 2- making nonessential amino acids 3- energy production 4- glucose production (critical) 5- conversion to body fat
Major sites of body fat
40%- skeleton muscle
30%- Skin/ blood
25%- body organs
Deamination process and where
removal of amine group (NHZ) enzymes that catalyst reaction called dreaminess and takes place in the liver
converts into urea for excretion in urine
higher intake= more protein
