2.1 Protein Study guide

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efrain12
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2.1 Protein Study guide
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2015-03-07 21:04:57
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Protein
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  1. Be sure not to confuse amino acids with proteins. Amino acids are building blocks of proteins) Amino acids are individual structures that make up a protein. They have a carbon, amine, and side group
  2. Do not need to memorize functional groups but be able to recognize an amino group)
    It is the part of amino acid that has NHHH
  3. Be able to discuss what differentiates one amino acids from another and some general differences between how they are categorized)
    They differ in their side chain which its what gives them their functional properties
  4. Be able to discuss what differentiates one amino acids from another and some general differences between how they are categorized) Categorized in one of 3 ways
    -may be grouped by molecules possessing similar structures

    -may be categorized by their charge balance & polarity

    -level of essentiality
  5. Memorize the 9 essential A.A and know what makes them essential)
    -phenylalanine

    -valine

    -threonine

    -methionine

    -tryptophan

    -histidine

    -isoleucine

    -leucine

    -lysine
  6. Memorize the 9 essential A.A and know what makes them essential)
    Our bodies cannot synthesize them endogenously
  7. Be able to discuss situations in which an amino acid may be conditionally indispensable or if one is described to you be able to recognize it as such)
    • organ failure, prematurity, genetic disorder may keep our body from making the precursors or enzymes necessary to synthesize nonessential AAs
    • *premature infants cannot synthesize cysteine, proline, arginine
  8. Be Able to say something about endogenous sources of AAs)  (2)
    -sloughed off mucosal cells (50 g/day)


    -digestive enzymes & glycoprotein (17g/day)
  9. Be able to discuss and identify the 4 phases of protein structure and roughly what differentiates them) Primary structure
    Amino acid sequence of the protein
  10. Be able to discuss and identify the 4 phases of protein structure and roughly what differentiates them) secondary structure
    Represents the coiling, folding, or bending of the AA sequence as the AA react to each other through hydrogen bonding
  11. Be able to discuss and identify the 4 phases of protein structure and roughly what differentiates them) Tertiary structure
    Refers to total 3d structure of PRO which gives its functionality
  12. Be able to discuss and identify the 4 phases of protein structure and roughly what differentiates them) Quaternary structure
    • result of multiple polypeptide chains interacting & coming together
    • *multiple proteins coming together to create one
  13. KNow the difference between HCL denaturing a protein vs an enzyme digesting a protein) how does HCL do it?
    HCL lowers pH and begins denaturing the tertiary & secondary structure of PRO causing uncoiling
  14. KNow the difference between HCL denaturing a protein vs an enzyme digesting a protein)
    Pepsin hydrolyzes the peptide bonds of the primary structure leaving large polypeptides, oligopeptides, & free AAs
  15. Understand and be able to discuss the role of zymogens and know why they are inactive until they reach their environment of action. You do not need to memorize the names of the zymogens of their resulting enzyme but it may make it easier to discuss if you learn at least one pair ) (2)
    Zymogens are inactivated version of enzymes

    • It is done this way on purpose to prevent activation of zymogens in pancreas which would lead to the enzymes digesting pro in the pancreas
    • *safety mechanism to make sure to get them to an environment that can handle them before activation
    • **pepsinogen -> Pepsin
  16. Know where protein digestion takes place and where it does not and roughly why)
    Small intestines & stomach
  17. Know where protein digestion takes place and where it does not and roughly why) stomach (3)
    -Gastric cells release gastric which stimulates HCL secretion

    -HCL lowers pH and begins denaturing tertiary and secondary structure of PROs causing to uncoil

    • -HCL converts pepsinogen to Pepsin which hydrolyzed peptide bonds of the primary structure
    • *leaves large polypeptides, oligopeptide, free AA to be dumped on small intestine
  18. Know where protein digestion takes place and where it does not and roughly why) Small intestine (3)
    • -Secretin stimulates secretion of bicarbonate, zymogens precursors of proteases, electrolytes, water
    • *secretin stimulated by presence of acidic chyme

    -each protease works on different type of amino acids

    -peptidases are located on brush border to promote further breakdown of A.A
  19. Know how far proteins have to be broken down before they can be absorbed into an enterocyte)
    Peptide chains need to be broken down to the level of dipeptides, tripeptides, & free A.As in order to be absorbed into enterocytes
  20. Be able to describe in detail the active/[passive mechanism of protein absorption into the enterocytes that you were taught ) (3 steps)
    1. Peptides are transported into enterocytes along with hydrogen in symport on apical

    2. Hydrogen is pumped out in exchange of sodium in antiport on apical

    3. Na/K ATPase pumps out Na in exchange for K to maintain a gradient on basolateral
  21. Have an understanding of the idea of amino acids need to compete for entry through receptors ) (2)
    Most of the transporters are Na symport to bring A.As in which was created by sodium potassium pump

    • All amino acids compete for shared transporters
    • *that's why not wise to supplement in one specific A.A
  22. Understand that the mechanisms of protein reception are in flux depending onto he amount of protein consumed or needed)
    • Protein receptor channels are subject to dynamic flux of up and down regulation according to the need of the body
    • *applies to all receptors in body
  23. Know where absorbed proteins and amino go next after being absorbed into the enterocyte)
    exit basolateral membrane to enter surrounding capillaries which leads them to the portal vein & then the liver for metabolism
  24. Summarize the overview of protein digestion) 6 steps
    -gastric cells release gastrin which releases gastric juices

    -HCL dentures proteins and converts pepsinogen to Pepsin which begins to digest proteins by hydrolyzing peptide bonds

    -partially digested proteins enter S.M to cause the release of secretin and cholecystokinin

    -pancreatic proenzymes convert to enzymes which digest polypeptides into tri/dipeptides and free AA

    - intestinal enzymes in the lumen of SM and within mucosal cells complete protein digestion
  25. Be able to discuss the main site of catablosim for AA vs the sites dedicated to BCAAs)
    Main site for essential AA is liver
  26. Be able to discuss the main site of catablosim for AA vs the sites dedicated to BCAAs)
    Are catabolized in muscle & heart cells
  27. transamination, how it works and its purpose) what is it?
    An amino group is transferred form one amino acid to the carbon skeleton of another amino acid

    • *original AA becomes carbon skeleton while the one receiving it becomes AA
    • *catalyzed by enzymes
  28. transamination, how it works and its purpose)
    Important for synthesis of many non essential AA
  29. Memorize the carbon skeletons for pyruvate, alpha ketoglutarate, oxaloacetate ) Pyruvate + NH3
    Alanine
  30. Memorize the carbon skeletons for pyruvate, alpha ketoglutarate, oxaloacetate ) A-Ketoglutarate + NH3
    Glutamate
  31. Memorize the carbon skeletons for pyruvate, alpha ketoglutarate, oxaloacetate ) Oxaloacetate + NH3
    Aspartate
  32. Be able to discuss the toxicity of NH3 and how the body handles it)
    Ammonia is toxic so body undergoes transamination b/c it provides a safe way to transport NH3 through system until it can be urinated as urea
  33. Know the difference between deamination & transamination
    deamination is when an amino group is removed without transfer to a carbon skeleton so it leaves an ammonia group out`
  34. Know what is special about a-ketoglutarate, glutamate, glautamine  (2)
    Alpha ketoglutarate can carry 2 ammonias as glutamine

    Play key role in the transport of ammonia for urea synthesis
  35. Urea cycle:  location of urea production and how it is eliminated from the body) (2)
    - location : liver

    -one run through cycle releases 2 NH3 in form of urea which we urinate
  36. 1-2 description of the purpose of urea cycle and what it does ready to go) (3)
    Urea cycle is how we get rid of ammonia

    Ammonia is passed through several transmiantions reactions until it can enter the urea cycle as aspartame


    It secretes 2 NH3 in form of urea through one cycle
  37. Be able to describe how TCA cycle interacts with the irea cycle to get rid of NH3 Discuss this is terms of transamination) the substrates (3)
    -oxaloacetate

    -fumarate

    -Co2
  38. Be able to describe how TCA cycle interacts with the irea cycle to get rid of NH3 Discuss this is terms of transamination) Oxaloacetate (2)
    Glutamate transminates OOA to aspartame to go into the urea cycle

    -OOA comes from TCA cycle
  39. Be able to describe how TCA cycle interacts with the irea cycle to get rid of NH3 Discuss this is terms of transamination) Fumerate (2)
    -in urea cycle, argino-succinate splits up into fumerate & arginine


    -fumerate then goes to TCA cycles to replenish ooa
  40. Be able to describe how TCA cycle interacts with the irea cycle to get rid of NH3 Discuss this is terms of transamination) CO2 (3)
    -CO2 produced from Acetyl COA during TCA cycles will be used to make carbonyl PO4

    -carbonyl Po4 will be used in urea cycle to join with ornithine to create citrullin

    -citrullin and aspartate join to make argino-succinate
  41. Be able to say something about what unregulated the urea cycle) (2)
    • -high protein increases expression of urea cycle enzymes
    • *exogenous proteins

    • -adrenal stress hormones increase expression of urea cycle enzymes
    • *endogenous protein
  42. Five uses for the metabolism of carbon skeletons)
    -energy

    -gluconeogenesis

    -ketones bodies

    -cholesterol

    -fatty acids
  43. Be able to discuss what qualities of an amino acid determine whether it will be ketogenic, gluconeogenic, or both (3)
    -Any carbon skeleton of the TCA cycle that can eventually turn into OOA are gluconeogenic

    -AAs which form acetyl coa or acetoacetate are ketogenic

    -BCAAs are both
  44. Why is acetyl coa not a gluconeogenic precursor) (3)
    Acetyl coa cannot lead to glucose production because its being carried by OOA through the tca cycle to be burnt off thereby releasing CO2.

    Acetyl coa is not an intermediate only being carried around

    Cannot become OOA
  45. Understand that if something can become acetyl coa that means it can become anything acetyl coa can become (fatty acid, cholesterol, ATP). SAme with an amino acid that can become pyruvate or ooa
  46. Thanksgiving turkey mythology) Turkey is frequently discussed as...
    High tryptophan food & this is often blamed for increase tryptophan levels in the brain which creates more melatonin production thus fatigue
  47. Thanksgiving turkey mythology) turkeys tryptophan content (2)
    Does not have much more tryptophan than any other meat

    • -100 grams has about .25 tyrptophan
    • *1% of total AA in turkey
    • *equivalent to what we usually find in other meats
  48. Thanksgiving turkey mythology) protein receptors at blood brain barriers are...
    Neutral so tryptophan must compete with all AA for entry which is not feasible due to only comprising 1% of AA
  49. Thanksgiving turkey mythology) tryptophan makes it in but
    Not because of the high content in turkey but bc of the enormous amount of crab consumption that occurs during thanksgiving
  50. Thanksgiving turkey mythology) what does a lot of cho consumption cause?
    -increase insulin signaling which leads to increased absorption of glucose and big bulky BCAAs into muscle cells thus decreases the competition at the blood brain barrier protein receptor allowing tryptophan to cross the blood brain barrier
  51. Thanksgiving turkey mythology) main point
    Due to high cabs not high in tryptophan in turkey
  52. 8 functional roles of protein)
    1. Tight junction proteins for cell adhesion

    2. signal receptors on cell membranes

    3. provide storage for some minerals

    4. Glycoprotein like mucus lubricate and protect epithelial linings

    5. proteoglycans make up the cornea of the eye, hyaluronic acid and chondroitin sulfate found in joints


    • 6. Fluid balancers like albumin creating osmotic pressures that draws water into vascular system
    • *decrease leads to edema

    7. Catalysts because they are enzymes and enzymes sped up reactions

    8. Immunoprotectors which are a full system of proteins for fighting foreign invaders and mobilizing immune attack
  53. Difference between biochemical theory and research prove reality) (2)
    In theory it may seem like a good idea but once its in action there are a lot more intricacies that one does not take into account.

    You can't single out a pathway bc its part of a collective processes involving many other pathways interdependent with one another
  54. Be able to discuss glutamine as a central player and the roles of glutamine in metabolism
    Glutamine can be deaminated to glutamate to be used for several purposes
  55. Be able to discuss glutamine as a central player and the roles of glutamine in metabolism (4)
    -ammonia transport

    -kidneys may use it for acid/base balance giving up its ammonia to absorb renal H to become ammonium for excretion

    -serves as fuel source for immune cells proliferation & function

    -primary source of energy in enterocytes
  56. Discuss glucose-palatine cycle in detail, its purpose, how it works)
    A way the body shuttles nitrogen to the liver for urea synthesis while conserving glucose during fasted state
  57. Discuss glucose-palatine cycle in detail, its purpose, how it works) (6)
    1. glycogenolysis frees glucose which is converted to private through glycolysis in muscle cells

    2. Glutamate transmiantes pyruabte to alanine

    3. Alanine travels to the liver from msuclecell

    4. Once in muscle, alanine transaminates a-ketogluterate to glutamate. Alanine is now pyruvate

    5. pryavte is put through gluconeogenesis to form glucose which is then released to msucoe cell

    6. Glutamate now has the nh3 and deaminates to release nh3 to urea cycle
  58. What happens to our protein store after protein ingestion and in starvation )
    We synthesize more protein than we catabolized
  59. What happens to our protein store after protein ingestion and in starvation ) (2)
    -we break down more protein than we synthesize

    -released into blood for use by other tissues
  60. Discuss protein catabolism and turnover. KNow lysosomal and proteasomal degradation) (3)
    -protein degradation is content process

    -25-35% occurs in msucel tissue

    -content degradation ensures constant influx of AA building block for synthesis of endogenous proteins
  61. Discuss protein catabolism and turnover. KNow lysosomal and proteasomal degradation) (2)
    Lycos some are organelle that digest macro and nucleic acids

    They destroy using acids
  62. Discuss protein catabolism and turnover. KNow lysosomal and proteasomal degradation) (2)
    Large hollowed structure with central cavity for protein degradation

    -shreds proteins
  63. Define complete protein, incomplete protein, limiting amino acid) (2)
    Contains all essential aa

    Mostly animal based foods
  64. Define complete protein, incomplete protein, limiting amino acid) (2)
    -do not contain all aa

    -mostly plant based
  65. Define complete protein, incomplete protein, limiting amino acid)
    The Essential AA in lowest concentration in a food
  66. Describe mutual supplementation)
    Combining legumes with grains to form a complete protein bc they provide what the other lacks
  67. Ear of protien
    .66 grams/kg bw
  68. Differences in protein digestibility and how this related to what you see on label) (1+2)
    -digestibility varies bw different protein sources

    • --animal 90-99%
    • --plant 70-90%
  69. Differences in protein digestibility and how this related to what you see on label) (2)
    -protein labels do not take protein quality of digestibility into account

    -the % daily value does take digestibility into account because uses PDCAAS which compares everything to casein in milk

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