RT Book, Section
A1 Kennelly, Peter J.
A1 Rodwell, Victor W.
A2 Rodwell, Victor W.
A2 Bender, David A.
A2 Botham, Kathleen M.
A2 Kennelly, Peter J.
A2 Weil, P. Anthony
SR Print(0)
ID 1160188876
T1 Proteins: Myoglobin & Hemoglobin
T2 Harper's Illustrated Biochemistry, 31e
YR 2018
FD 2018
PB McGraw-Hill Education
PP New York, NY
SN 9781259837937
LK accesspharmacy.mhmedical.com/content.aspx?aid=1160188876
RD 2024/04/19
AB OBJECTIVESAfter  studying  this  chapter,  you  should  be  able  to:Describe  the  most  important  structural  similarities  and  differences  between  myoglobin  and  hemoglobin.Sketch  binding  curves  for  the  oxygenation  of  myoglobin  and  hemoglobin.Identify  the  covalent  linkages  and  other  close  associations  between  heme  and  globin  in  oxymyoglobin  and  oxyhemoglobin.Explain  why  the  physiologic  function  of  hemoglobin  requires  a  sigmoidal  rather  than  hyperbolic  O2-binding  curve.Explain  the  role  of  the  distal  histidine  on  the  ability  of  hemoglobin  to  bind  carbon  monoxide  (CO).Define  P50  and  indicate  its  significance  in  oxygen  transport  and  delivery.Describe  the  structural  and  conformational  changes  in  hemoglobin  that  accompany  its  oxygenation  and  subsequent  deoxygenation.Explain  the  role  of  2,3-bisphosphoglycerate  (BPG)  in  oxygen  binding  and  delivery.Explain  how  the  Bohr  effect  enhances  the  ability  of  red  blood  cells  to  transport  CO2  and  deliver  it  to  the  lungs.Describe  the  structural  consequences  to  hemoglobin  S  (HbS)  of  lowering  Po2.Identify  the  metabolic  defect  that  occurs  as  a  consequence  of  α  and  β  thalassemias.