Hemoglobin & Myoglobin

Hemoglobin& Myoglobin

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Unformatted text preview: globin in blood would not be able to carry out the functions. 2/8 and 2/11/13 MCB 2000 Lecture 6 hemoglobin - 2 alpha and 2 gamma changes - during developemnt it matures - repleace the gamma chains with beta c hains - in fetal hemoglobin have sub of one of the amino acid for a polar amino acid (see next page) can bind 23 BPG as well - fetus getting oxygen from mother - tigher binding 6$&"*$9*NLKC<(047$047$%&-5"231"*DNLKC<=^E*()* $F-%")*'();()%*1$*7"#$%&$'()* when oxygen binds the 2-3 BPG will come off - the binding of 2-3 BPG will promote the binding of oxgyen to release oxygen to tissues Hemoglobin - trasnport protein - allosteric properties and cooperativity= s s haped curve the 2-3 biphsophoglycerate will bind to the central c avity because neg charged - 2-3 BPG dont see it when hemolgobin binds oxygen - 2-3 BPG stablizies the T state - promotes the release of oxygen from hemoglobin black without 23BPG and pink with itwithoutand 2/11/13to oxygen more tightly acts more like myogblin ( RLecture 6 2/8 it hangs on MCB 2000 s tate) *********** Prompots the release of oxygen - shift towards the right 2,3-BPG stabilizes the T state Molecules that hemoglobin can bind to o- 2-3 BPG - by product of glcoysis - hemoglobin in RBC - has no mitochondria - cant carry out phosporlation - cant do a lot of ATP - in RBC - will have a lot of the intermediate made highly neg. charged - it binds in the centeral cavity of hemoglobin P731*1-4"*$9*)$)5$:3&")1*()1"2351($)0* 013'(&(A"*NLKC<=^*'();()%*()*17"*5")123&* 53:(1-*V* 2/8 and 2/11/13 In the central cavity - the side chains of amino acid - the electrostatic interaction stablizing the binds of 2-3 BPG- the s tructure is neg - needs to electrostatic - all the amino acids are basic can contribute a postivie charge - this stucture is deoxy hemoglobin - you can see the central cavitiy. MCB 2000 Lecture 6 R7"*<$72*_99"51H*** 17"*2"%/&31($)*$9*$F-%")*'();()%*1$*!'*'-*!Q* 3);*[UN* * Hemoglobin binds protons and CO2 - Bohr effect will relate to the binding of protons (H+) ability of hemolgobin release oxgyen in presence of protons and CO2 - where will this be found? - metablizing acitivity in tissues -reginos with high metablic acvitity will fi nd protons and CO2 and will promote the r elaease of oxygen - CO2 will diffuse from tissue into the blood and will enter the red cell and combind with water - the reaction can happen spontaneslouly - form carboin and dissoicate into bicarbonate and a proton - and the proton will effect the realese of oxygen ties the relationship between buffer capacity and oxygen effetiviety 2/8 and 2/11/13 MCB 2000 Lecture 6 How does H+ (pH) and CO2 affect O2 binding to Hb? Hb carries 2 end products of respiration: 2/8 and 2/11/13 CO2 diffuses over longer distance - ends the capillary vessel and dissolved in water and taken up by the RBC - this reaciton happens without an enzyme but...
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This note was uploaded on 09/17/2013 for the course MCB 2610 / 200 taught by Professor Feldman during the Fall '12 term at UConn.

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