[BIOCHEM} Peptides & Proteins

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Chemistry

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130 Terms

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Peptides and proteins
polymers of amino acids joined by peptide bonds
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Peptide Bonds
a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O)
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Amide Bond
other term for Peptide bond
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Peptide bonds
covalent bonds between amino acids in a peptide
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Amino Acid
is covalently linked together by the formation of an amide bond between a-carboxyl group of one amino acid with another a-amino group of another amino acid
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Left to Right
direction of how Peptide Sequences are written
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-COO
carboxyl group
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NH3+
Amino group
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Dipeptide
peptide that consists of 2 amino acids
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Dehydration Reaction
the process of removing or loss of water from the molecule or ion
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Peptide
has a lower molecular weight compared to protein
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Peptide
consist less than 50 amino acids
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Protein
molecules with more than 50 amino acids
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Protein
consist of one or more polypeptide chains
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Protein
is the heaviest among peptides, oligopeptides, and polypeptides
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Oligopeptide
a polymer consisting of 2 to 10 amino acids (less than 10 and around 2)
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Tripeptide
peptide that has 3 amino acids
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Polypeptides
peptide that have more than 10 amino acid residues (more than 10, below 50)
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9
# of amino acids of Oxytocin
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9
# of amino acids of Vasopressin
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51
# of amino acids of Insulin
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84
# of amino acids of Parathyroid hormone
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Oxytocin
hormone secreted by the posterior pituitary gland; stimulates contractions of the uterus and ejection of milk
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Altruistic behavior
selflessness characteristic of an individual
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Vasopressin
- responsible in the regulation/control of blood pressure and blood volume
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Vasopressin
hormone that stimulates the kidneys to retain water when a person is dehydrated
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Insulin
hormone that facilitates entry into insulin-sensitive cells
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Parathyroid hormone
hormone that functions in regulating blood calcium levels
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Enkephalins
- are pentapeptides neurotransmitters produced by the brain
- responsible for binding receptor sites in the brain to reduce pain
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Met-enkephalin & Leu-enkephalin
best known Enkephalins
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Glutathione
is significant for its antioxidant property
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Antioxidant
are substances that protect the cells against free radicals
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Glu-Cys-Gly
the tripeptide present in high levels of most cells
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Proteins
most important out of all biological compounds
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Proteios
greek word for protein; meaning "of first importance"
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400-500
# of amino acid residues in common proteins
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40-100
# of amino acid residues in small proteins
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Monomeric
a protein that contains one polypeptide chain
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Multimeric
a protein that contains two or more polypeptide chains
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Simple proteins
proteins that are entirely made up of Amino acids only
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Albumin
protein that is soluble in water; soluble in diluted aqueous salt sol'n and heat coagulable
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Globulin
protein that is insoluble in water, soluble in aqueous salt solution, and heat coagulable
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Glutelin
protein that is soluble in dilute acid and alkalies and is heat coagulable
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Prolamine
an alcohol soluble protein
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Albuminoid or Scleroprotein
the least soluble protein
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Protamine
- the simplest and basic protein, is soluble and dilute ammonia, acid, and alkali
- is found in spermatozoa
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Histone
- basic protein and is soluble and very dilute acid
- found in combination with DNA
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Conjugated Proteins
proteins that are made up of amino acids and other substances
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Prosthetic Group
other term for Conjugated proteins
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Nucleic Acid
prosthetic group of Nucleoprotein
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Carbohydrates
prosthetic group of Glycoprotein
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Phosphoric acid residues
prosthetic group of Phosphoprotein
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Chromoprotein
the prosthetic group that gives color
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Lipid
prosthetic group of Lipoprotein
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Metals or Minerals
prosthetic group of Metalloprotein
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Derived Proteins
the degradation products obtained by the hydrolysis of natural proteins with acids, alkalis, and enzymes
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Primary Derived
proteins derived from simple or conjugated proteins by physical or chemical means
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Denatured Protein
other term for Primary derived protein
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Secondary Derived
protein formed through progressive hydrolytic product of protein hydrolysis
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Protein Hydrolysis
aims to break down the peptide bonds and to increase the free amino acid and carboxyl groups
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Fibrous Proteins
proteins that are
- elongated, asymmetrical
- tough
- insoluble in water
- arranged around a single axis to form a fiber
- involved in structural functions
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Collagen
most abundant fibrous protein in the human body (25%)
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Keratin
a fibrous scleroprotein that occurs in the outer layer of the skin and in horny tissues such as hair, feathers, nails
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Globular Proteins
proteins that are
- circular and symmetrical
- involved in mobile and dynamic functions
- soluble in water
- for transport purposes (MAIN PURPOSE)
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Primary Protein Structure
describes the linear sequence of amino acids in the polypeptide chain
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Secondary Protein Structure
- localized regional structure of a protein
- formed due to the hydrogen bonds between peptide bonds
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Tertiary Protein Structure
protein structure that shows the overall shape of the protein
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Quaternary Protein Structure
protein structure that shows the interactions between proteins
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Primary Protein Structure
knowt flashcard image
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Secondary Protein Structure
knowt flashcard image
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Tertiary Protein Structure
knowt flashcard image
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Quaternary Protein Structure
knowt flashcard image
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20^n
the number of peptides possible for a chain of n amino acid
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20
# of peptides for each amino acid
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Leu, Ala, Gly, Ser, Val, Glu
most abundant amino acids in proteins
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Trp, Cys, Met, His
rarest amino acids in proteins
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Pauling & Corey
first one to proposed the 2 secondary structures of protein:
~ alpha-helix
~ beta-sheet
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Alpha Helix
~ rod-like structure (phone cord)
~ amino acid R groups extend OUTWARD from the helix
~ main chain atoms on the INSIDE
~ helices can be right or left-handed
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Beta-Pleated Sheet
~ second most commonly occurring secondary structure of protein
~ R groups lie ABOVE/BELOW the zigzagging planes of the pleated sheet and are nearly PERPENDICULAR to them
~ second most commonly occurring secondary structure of protein
~ R groups lie ABOVE/BELOW the zigzagging planes of the pleated sheet and are nearly PERPENDICULAR to them
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Antiparallel beta-sheet
- neighboring H-bonded polypeptide chains run in OPPOSITE DIRECTION
- more stable
- 2 linear polymers of AA run in opposite direction
- neighboring H-bonded polypeptide chains run in OPPOSITE DIRECTION
- more stable
- 2 linear polymers of AA run in opposite direction
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Parallel beta-sheets
~ H-bonded extend in the SAME DIRECTION
~ the adjacent strands run in the SAME DIRECTION
~ H-bonded extend in the SAME DIRECTION
~ the adjacent strands run in the SAME DIRECTION
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Tertiary Protein Structure
- results from the interactions between amino acid side chains ( R grps) that are widely separated from each other
- have WATER-SOLUBLE proteins fold into compact structures with NONPOLAR CORES
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Quaternary Protein Structure
- highest level of protein organization
- polypeptide chains (subunits) maybe identical or different
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Dimer
protein structure that consist of 2 polypeptide chains/subunits
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Trimer
a polymer consisting of 3 polypeptide chains
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Tetramers
a polymer consisting of 4 polypeptide chains
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Pentamer
a polymer consisting of 5 polypeptide chains
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Protein Folding
- process by which a protein structure assumes its functional shape or conformation
- a process where a protein chain acquires its 3-dimensional structure
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Chaperones
assist in preventing the protein from associating to inappropriate molecules
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Denaturation
the process of destroying the native conformation of a protein by chemical or physical means
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Gly
Glycine
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G
Glycine
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Ala
Alanine
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A
Alanine
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Val
Valine
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V
Valine
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Leu
Leucine
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L
Leucine
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Ile
Isoleucine
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I
Isoleucine