1. Introduction

The sequencing of amino acids into protein follows biophysical structural conformation in space-time. The sequencing of amino acids into protein can be determined by structural conformations in normal alpha and beta chains in human hemoglobin that also aligned to p53 protein molecule. A generalized structural matter would be applicable to sequencing of all kind of proteins. The generalizations are as follows:

1. The molecular point ‘197’(val-p53) is a fundamental structural parameter where 197*0.0019 = 2*0.1872 in space-time. [1]

2. The molecular point of amino acids are related to the core values(C_v) or hidden time of corresponding amino acids in the structure e.g. Met C_v = 149*0.0019 – 0.2124 = 0.0707.

3. The protein molecules would possess structural suppression.

4. The protein molecule bisects on appearing ‘367’ (earth-moon time curvature), if not further amplified since 183*0.0019 = 0.3477(lunar time limit) while 367 = 183 + 184.

5. Glutamine(146.1451) is a vital amino acid acts towards structural conformation.

The understanding of amino acid sequencing is needed as a cancer perspective while it would not be feasible to reinstate mutated protein. As p53 and hemoglobin chains are co-related, sickle-cell-anemia and cancer would thus cause a syndrome.

2. Discussions

The sequencing of amino acids into protein:

The human normal hemoglobin comprises two identical alpha and beta chains are anti-parallel chains showing structural conformations. The causes of two identical alpha hemoglobin(R-141 amino acid long) is to bisection of terminal amino acid(R282-p53) due to appearing ‘367’ curvature of time where 367 = 282 + 85(suppression) as well as bisection of oxy-time(0.0304) and for beta-chain, 368 – 146 = 222 = 393(p53) – 171. The molecular point 146 occupied by His in beta chain of hemoglobin while 146-trp in p53 shows structural conformation i.e. 0.1615(trp core values) – 0.1393(his core values) = 0.0222 = 222 = 257 – 35 where 146(trp-p53) + 111 = 257.

Accordingly, 368 + 292 = 660 = 393 + 267 = 327(tyr-p53) + 3*111 where 333 – 146 = 187 = 197 – 10 where 292 – 282 = 10.

The structural conformation tends to 54-gln and 59-lys from terminal of alpha and beta chains of hemoglobin with 146 – 141 = 59 – 54 = 5 values difference. The molecular point equipoised for alpha and beta chains and ultimately single molecular point difference where glutamine plays an important role.

Mathematically, 0.1494(glu core values, E6-beta) – 0.1323(gln core values) = 0.0171 = 171 where 393(p53) = 222 + 171 in the bi-folded structure.

There is no basic difference between glu(6-beta) and asp(6-alpha) except 0.1495(asp core values) – 0.1494(glu core values) = 0.0001 = 1. Now, 222 – 171 = 51 = 1545(tyr core values) – 1494(glu core values) and suppression values 85 = 51 + 35 with one molecular point difference about commonly seen.

Cys-Glu perspectives in hemoglobin chains:

Since oxy-time(0.0304 = 16*0.0019) is bisected at p53 terminal point(282), cys-glu structural symmetry is applicable to this.

Now, 147.1299(glu) + 121.1590(cys) = 268.2889 where 152*0.0019 = 0.2889 according to formula T(time) = M(mass)*0.0019.

Or, 0.2889 – 0.0268 = 0.2621(138) pre-transitional values gives 268 = 138 + 130.

Now, 130 + 152 = 282 = 141*2(alpha chains) and 138 + 152 = 290 = 146*2(beta chains) with 0.0002 adjustable time difference. Since alpha and beta chains are oppositely directed, 146 + 29(approaching value to lunar gravity found as spots in chromatography) = 175 = 327(tyr) – 152 and 122 + 29 = 152 - 1 in the structure.

Cys’s are found in positions 93 and 112 in beta chain shows alpha and beta chains interactions i.e. 93 + 29 = 122 and 112 + 29 = 141. Conversely, 122 + 104(cys-alpha or gln-p53) = 226 = 367 – 141 = 292(lys-p53) – 66(t-RNA ‘distance of constancy’ factor).

Again, 0.1323(gln core values) – 0.0709(cys core values) = 0.0614 where 0.0707(met core values) – 0.0614 = 0.0093 = 93. The met and cys having 0.0002 core values difference.

Met is found in position 55(Hb-beta chain) and in positions 32, 76(Hb-alpha chain).

Structurally, 55 + 29 = 84 = 177 – 93 and 122 + 32 = 154 = 183(lunar time) – 29 = 100 + 55 and 122 + 76 = 198 = 227 - 29 with one molecular point difference that showing a ‘100’ factor in methionine derived from 803(half of lunar gravity) – 703(met core values with 0.0004 adjustable time difference) = 100 and 1254(66) – 551(29) = 703(37) avoiding decimals. Consequently, 136(gln-p53) is associated with met where 3477(183-lunar time) – 803 = 2674 = 2774(146) – 100 avoiding decimals.

The cys and met are differentiated by 0.0002 core values while cys is incorporated into tyr can be found in context of oxy-time(0.0304).

Trans-activated sequencing in p53:

In p53, 1872(197) – 1545(tyr core values) = 327(tyr) = 220(tyr) + 107(tyr) and 327 – 130 = 197 = 131 + 66 and 131(leu vertical time)*0.0019 = 0.2489 where 2489 – 617(V617F) = 1872, avoiding decimals. The values 1545 – 1254(66) = 291(lys) = 184 + 107(tyr). Accordingly, 0.1545(tyr core values) – 0.0893(lys core values) = 0.0652 = 1975(met pre-transitional value) – 1323(gln core values) = 652 = 361 + 291 since 0.1254(66) – 0.0893 = 0.0361 = 361 are structural matters. Biophysically, Tyr and Lys is very systematic since AAA(405) – UAC(358) = 47(a fundamental value) and conversely Met + 29(0.0551) = Phe.

Here, 652 = 552 + 100 = 617 + 35 = 2*326(terminal mutation at C843T R282W) [2] and 1494(glu core values) – 652 = 842 where 367 + 103 = 469 + 1 and 652 – 183(lunar time) = 469(G469T V157F) and also1872 – 1494 = 378(TTT) would cause directional conflicts whenever instability exists. It is seen 327*3 = 981 = 844 + 137 = 2831(149) - 1849 where 844 – 707(met core values) = 137 and 1451 – 982 = 469 are cancer components in biophysical structure.

Furthermore, 327(tyr) + 291(lys) = 618(V617F) and 327 – 156(V157F) = 171 = 136 + 35 where 327 – 291 = 36 = 30 + 6(glu-beta) in biophysical structure that indicates cancer and sickle-cell-anemia are co-related and would be oppositely active. What is the relation between cell de-oxygenation and tumor formation?

Trp positioning in p53 and hemoglobin chains:

Trp found at 23, 53, 91, 146 positions in p53 while 1872 – 1615(trp core values) = 257.

Now, 257 – 146 = 111 = 393(p53) – 282; 257 – 91 = 166 = 393 – 227 where 368 – 227 = 141; 257 – 53 = 204 = 393 – 189 where 189 = 282 – 93 and 146 = 93 + 53; 257 – 23 = 234 = 393 – 159 where 93 + 66 = 159 with 0.0002 time difference.

Again, 37(trp-beta) + 29 = 66 and 257 – 66 = 191 = 282 – 91(trp-p53); 121 + 14(trp-alpha) = 135 = 257 – 122.In directional context of alpha and beta hemoglobin, 29 +146 = 175 = 327(tyr) – 152 while 121 + 141 = 262 = 291(lys) – 29.

3. Conclusions

The clarification of hemoglobin alpha and beta anti-parallel chains structure is biology in space-time. The sequencing of particular amino acids is clarified in biophysical structure. There should be a generalized structure for time motivation forming the sequence of proteins. The cancerous arena has been shown lies in fundamental biophysical structure goes detrimental under structural mutations.