Proteins part 1 Flashcards
Proteins contains how many percent of cell’s dry weight?
50-70%
Most abundant macromolecules in the body
Proteins
Proteins are expressed in?
g/dL
What element differentiates protein from other macromolecules.
Nitrogen
Proteins are synthesize in the?
Liver
These are produced in the plasma cells
Immunoglobulins
positively or negatively charged.
Amphoteric
TRUE OR FALSE:
Proteins are water soluble and amphoteric?
TRUE
What is the charge of CHON in Alkaline pH?
Negative
What is the charge of CHON in Acidic pH?
Positive
What type of bond holds the AA together?
Peptide bonds / Amide linkages
Give 3 essential AA
Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan and Valine
Refers to the identity and specific order of amino acid residues in the polypeptide chain (amino acid sequence)
Primary structure
Determines the overall shape of the protein
Primary structure
Refers to the sequence of AA in a peptide or protein
Primary structure
Conformation of the segments of polypeptide chain.
Secondary structure
What are the sheets that composes the secondary structure?
Alpha-helix and beta-pleated sheet
What type of bond maintains the secondary structure?
Hydrogen bond
Intramolecular folding of the polypeptide chain into a compact 3-dimensional structure.
Tertiary structure
This refers to the denaturation of proteins that occurs when temperature change or in the presence of organic solvents or reagents that may change the tertiary structure.
Unfolding
What type of bond maintains tertiary structure?
Covalent Disulfied bond
Association of several polypeptide subunits into a larger “oligomeric” aggregate unit.
Quaternary structure
Incorporation of 2 or more polypeptide chains or subunits into a larger unit
Quaternary structure
What are the examples of Quaternary structures?
Creatine kinase, Lactate dehydrogenase, and Hemoglobin
How many subunits does Hemoglobin has?
4
Proteins can be differentiated based on?
A. Differential solubility
B. Molecular size
C. Molecular mass
D. Electrical charge
E. SURFACE ADSORPTION
– CHON are affected by pH, ionic strength, temperature and dielectric constant.
Differential solubility
pH where proteins have no net charge
Isoelectric point
ions that has 2 different charges but net charge on the molecule is ZERO.
Zwitterions
Accomplished through ultracentrifugation or dialysis
Molecular size
Can be accomplished through mass spectrometry
Molecular mass
Can be accomplished using ion exchange chromatography and electrophoresis.
Electrical charge
Can be done using chromatography
Surface adsorption
Between serum and plasma, which one contains Fibrinogen?
Plasma
Due to the absence of Fibrinogen in serum, the total content decreases into how many percent?
4%
