Busm Biochemistry Hgb Interactions Quick

Front 1

fractional saturation of mgb equation?

Back 1

Front 2

Helix of the histidine that ligates heme( the 5th coordination site)?
residue # in mgb, b-chain, a-chain?

Back 2

Helix F8

mgb = residue 93
hgb b-chain = residue 92
hgb a-chain = 87

Front 3

6th coordination site in the deoxy state? helix and residue numbers?

Back 3

helix E7

mgb = residue 64
hgb b-chain = residue 63
hgb a-chain = residue 58

Front 4

fractional saturation of HGB

Back 4

Front 5

Hill equation of HGB

Back 5

Front 6

The _____ subunits of hgb may or may not be identical while the ____ subunits are identical

Back 6

alpha = maybe identical

beta = identical

Front 7

What residue facilitates the rotation of the alpha/beta dimer when o2 binds?

Back 7

His F8

Front 8

Deoxy/T-state stabalizing interactions?

Back 8

-C-terminius of Beta HIS lies on top of helix C in alpha and interacts with Asp 94 of the same β2 by charge-charge interaction and with Lys 40 of the α1 through charge-charge interactions
-N-terminal (NH3 grp) residue of α1 interacts with the guanidinium group of carboxyl terminal residue (Arg) of α2 via charge-charge + Cl-
-guanidinium group of the C- terminal residue Arg141 of the α1 interacts with Asp126 of α2
-Tyr 140 of α1 hydrogen bonds to the carbonyl group of Val 93 in the same
subunit. Similarly, Tyr145 in the β subunit forms a hydrogen bond with the carbonyl group of Val98.

Front 9

Bohr effect in terms of specific residue

Back 9

excess protons protonate C terminus B2 146 His and stabalize the deoxy/T state

Front 10

where does carbamation happen? effect?

Back 10

carbamation happens N-terminus and stabalizes the salt bridge formation between alpha and beta chains

Front 11

what residue is replaced by ser in fetal gamma subunit? effect?

Back 11

his 143 is replaced by ser in fetal gamma subunit = positive charge replaced by negative = repels BPG = fHgb has less affinity for BPG = fHgb has higher O2 affinity

Front 12

amino acid residues involved in binding 2,3BPG are

Back 12

Lys82, His143, His2, and the N-terminal amino group of the β- chains?

Front 13

How many residues in alpha chain of HGB?

How many residues in beta chain of HGB?

Back 13

alpha = 141

beta = 146

Front 14

the plane of ______ and ______ is rotated to avoid collision with the heme

Back 14

valFG5 and leuFG3

Front 15

relative rotation of alpha-beta units in hgb?

Back 15

15degrees

Front 16

His F8 function in hgb?

Back 16

proximal his that binds Fe(II)

Front 17

His E7 function in hgb?

Back 17

Distal histidine, protects the heme and forces O2 to bind at an angle

Front 18

Phe CD1 function in hgb?

Back 18

Heme contact

Front 19

Leu F4 function in hgb?

Back 19

Heme contact

Front 20

Gly B6 function in hgb?

Back 20

Allows approach of B and E helices

Front 21

Pro C2 function in hgb?

Back 21

Terminates the helix

Front 22

Tyr HC2 function in hgb?

Back 22

hydrogen bond between H and F helices

Front 23

On assuming the R state the iron moves down ____ angstroms into the same plane as the porphyrin.

Back 23

0.6A

Front 24

_______________ interacts with Asp of the same β2 by charge-charge interaction and with Lys 40 R-group of the α1 through charge-charge interactions.

Back 24

C-terminus of β2 (His146) interacts with Asp of the same β2 by charge-charge interaction and with Lys 40 R-group of the α1 through charge-charge interactions.

Front 25

C-terminus of β2 (His146) interacts with _____ of the same β2 by charge-charge interaction and with_______ of the α1 through charge-charge interactions.

Back 25

C-terminus of β2 (His146) interacts with Asp of the same β2 by charge-charge interaction and with Lys 40 R-group of the α1 through charge-charge interactions.

Front 26

In deoxy Hb, the _____________________________ interacts with the carboxyl terminal residue Arg guanidinium group of α2, via charge-charge interactions. This involves a ____________.

Back 26

In deoxy Hb, the amino group of the Val N-terminal residue of α1 interacts with the carboxyl terminal residue Arg guanidinium group of α2, via charge-charge interactions. This involves a chloride bridge.

Front 27

In deoxy Hb, the amino group of the Val N-terminal residue of α1 interacts with the ___________________, via charge-charge interactions. This involves a chloride bridge.

Back 27

In deoxy Hb, the amino group of the Val N-terminal residue of α1 interacts with the carboxyl terminal residue Arg guanidinium group of α2, via charge-charge interactions. This involves a chloride bridge.

Front 28

In deoxy Hb, the ___________________________ of the α1 interacts with Asp126 of α2 and is similar in a2a1.

Back 28

In deoxy Hb, the guanidinium group of the C- terminal residue Arg141 of the α1 interacts with Asp126 of α2 and is similar in a2a1.

Front 29

In deoxy Hb, the guanidinium group of the C- terminal residue Arg141 of the α1 interacts with ____________________________

Back 29

In deoxy Hb, the guanidinium group of the C- terminal residue Arg141 of the α1 interacts with Asp126 of α2 and is similar in a2a1.

Front 30

In deoxy Hb, _________ hydrogen bonds to the carbonyl group of Val 93 in the same subunit. Similarly, _____________ subunit forms a hydrogen bond with the carbonyl group of Val98.

Back 30

In deoxy Hb, Tyr 140 of α1 hydrogen bonds to the carbonyl group of Val 93 in the same subunit. Similarly, Tyr145 in the β subunit forms a hydrogen bond with the carbonyl group of Val98.

Front 31

In deoxy Hb, Tyr 140 of α1 hydrogen bonds to the ____________ in the same subunit. Similarly, Tyr145 in the β subunit forms a hydrogen bond with _______________________

Back 31

In deoxy Hb, Tyr 140 of α1 hydrogen bonds to the carbonyl group of Val 93 in the same subunit. Similarly, Tyr145 in the β subunit forms a hydrogen bond with the carbonyl group of Val98.

Front 32

In deoxy Hb, Tyr 140 of α1 hydrogen bonds to the carbonyl group of Val 93 in the ___________. Similarly, Tyr145 in the β subunit forms a hydrogen bond with the carbonyl group of Val98.

Back 32

In deoxy Hb, Tyr 140 of α1 hydrogen bonds to the carbonyl group of Val 93 in the same subunit. Similarly, Tyr145 in the β subunit forms a hydrogen bond with the carbonyl group of Val98.