CC1 protein

• amino acids are simple organic compounds that serve as the building blocks of protein
• n terminal end of the amino acid
• c terminal end of the carboxyl group
• the amino group of one amino acid can be covalently linked with the carboxyl group of another amino acids forming a peptide bond
• when a chain of amino acids is linked by peptide bonds it is known as a polypeptide
• proteins consists of the element carbon, oxygen, hydrogen, nitrogen and sulfur
• primary structure refers to the number, type and sequence of amino acids in the polypeptide chain
• secondary structure refers to commonly formed arrangements stabilized by hydrogen bonds between nearby amino acids within the protein .
• secondary structure the polypeptide chain wind to form alpha helixes and beta sheets through the formation of hydrogen bonds between CO and NH groups of peptide bonds
• tertiary structure the coiled polypeptide chain folds upon itself to form a 3D structure through the interactions of the r group of the amino acids.
• quaternary structure two or more folded polypeptide chain binds to each other through hydrogen bonds and electrostatic interaction to form a functional protein
• simple proteins polypeptides composed of only amino acids
• globular proteins - symmetrical, compactly folded polypeptide chain
• fibrous proteins - elongated, asymmetrical polypeptide chain
• conjugated proteins - composed of protein and non protein comments; prosthetic group are commonly metal, lipid and carbohydrates in nature
• metalloproteins - metal prosthetic grp
• lipoproteins - lipid prosthetic grp
• glycoproteins - 10-40% carbohydrates attached
• mucoproteins - >40%carbohydrates attched
• nucleoproteins - DNA or RNA nucleic acids attached
• proteins can be broken down into amino acids that can be used in the citric acid cycle to produce energy - energy production
• maintain the colloidal osmotic pressure between diff body compartment - water distribution
• the ionizable r grp of the individual amino acids of protein provide buffering capacity by binding or releasing h+ ions as needed - buffer
• binding the proteins to hormones, free hemoglobin, lipids, drugs, calcium, unconjugated bilirubin; allows the movement of these and other molecules in the circulation - transporter
• proteins that protects the body against foreign invaders - antibodies
• functions as receptor for hormones so that the hormonal messages can activate cellular components, some hormones are protein in nature - cellular protein
• maintain structure of body parts - structural proteins
• catalysts that accelerate chemical reaction - enzymes
• some cytokines released at the site of injury or inflammation cause the liver to increase synthesis or the acute-phase reactant protein
• proteins that decrease in concentration - negative acute-phase proteins
• are hormonal antibodies produced in response to foreign antigens for the purpose of destroying them
• total protein range - 6.5-8.3g/dL
• albumin range - 3.5-5.0g/dL
• hypoproteinemia - urinary loss, GI tract, inflammation, liver disorder, malnutrition, inherited immunodeficiency disorder and extensive burns
• hyperproteinemia - dehydration, increased protein production associated with monoclonal and polyclonal gammopathies and chronic inflammatory disease associated with paraprotein production
• prealbumin - aka transthyretin, indicator of nutritional status and is one of the proteins that transport thyroid hormones
• prealbumin decrease in liver disorder, inflammation, malignancy and poor nutrition
• prealbumin incresed in steroid therapy, chronic renal failure and alcoholism
• albumin - synthesized in the liver and has the highest concentration of all plasma proteins. it binds many analytes for transport in blood
• albumin decreased in liver disorder because of decreased production, gastrointestinal disease associated with malabsorption, muscle-wasting disease, severe burns caused by loss, renal disease caused by loss starvation and malnutrition