Introduction

The main function of proteins in living organisms including human are : (a) controlling of almost all the biological reactions, and (b) to maintain a deep relationship through their structure and function which are related to the development of life ¹ .  In one side  it is considered that neighboring atom formation ² are the main structural basis  in many biological systems while in other side the attached hydrogen atoms take an active part in playing biological functions, such as mechanism of enzyme production ^3,4 . In deep sense, the precise location of this hydrogen atoms is very much crucial  in order to understand the physics of origin or mechanism related to the concerned biological problems by maintaining a relationship with solid state physics^5,6 .

The unknown crystal structure , in general, is resolved through the conventional method , i.e. the X-ray diffraction technique ^7,8 but the problem arises due to the interaction of X-rays with the electrons of the atoms located inside the crystal structure.  An alternate is to consider heavy atoms having neutrons with its isotropic form or other so that  the determination of the crystal structure is possible based on the relative position of a hydrogen atom located with reference to the known presence of relatively heavy atoms ^9,10. Therefore, control of physical parameters are essential for obtaining accurate result. Various methods have been developed in this regard by controlling the physical parameters such as the temperature ¹¹, hydrodynamic field ¹², electric field ¹³, magnetic field ¹⁴ and electromagnetic field ¹⁵. Out of these, magnetic field method has a great potential for understanding the protein crystal structure and its growth.

Although it is uncertain yet scientists believe that the knowledge of  protein were known during the period in the 19^th and early 20^th Century. In 1938 Berzelius first cointed the term “Protein” but remained unpopular under the influence of more popular terms like “proteid”, “albumineous”, “colloids” on that time. Looking back into the past the available literature indicates that in 1840 Friedrich Ludwig Hünefeld first observed protein crystal serendipitously in a sample of dried menstrual blood sticked between glass plates used for experiments in his laboratory (figure 1B ) ¹⁶ .

In fact, the word “Protein” is derived from the Greek word ‘Proteios’ which means primary / primary importance because proteins are the most important chemical  substances which are essential for growth, repair and development of life. These proteins have been found in all living cells implying that they occur in every part of the body and form the fundamental basis of structure and functions of life.  For example, in human body skin, hair, haemoglobin, nails, enzymes and cells, etc.  all are made of proteins.

However, through gradual studies protein crystallization area developed a lot and it has become an input part of our life, in particular through which we visualize the objects in the world.

Materials and Methods

The Birth of Biocrystallogenesis Initially,  protein crystal was confined its purification and then turned as instrumental tool to demonstrate its catalytic activities in the form of “enzyme” that resides with the protein itself. In the 19^th Century the most of the crystalline proteins (i.e. haemoglobins and albumins) which were considered as pure substance. Because of their availability in the micro-scale. But in 1934 a breakthrough occurred in this field when John D. Bernal and Dorothy Crowfort Hodgkin (see the review Parui 2024 ¹⁹ ) described the  secret  structure / pattern inside the protein first time through X-ray diffraction. This opened a new era in chemistry and physiology as biocrystallogenesis. Below a few landmarks are mentioned in protein crystallization.

Figure 1 : shows photographs of protein crystallization. (A) Crystals of excelsa exelsin from the Brazil nut (left) and of Avena sativa avenalin from oat kernels (right) 20: Click here to view Figure

Protein Crystallization in Living Cells

Protein crystallization in living cell was observed surprisingly as an evidence of phenomenon for recombinant protein. It  means that  this micrometer-sized can be used for structural biology. For example, this in cellulo crystallization could offer us a new possibilities that do not crystallize under normal conventional approach. In other words, this unknown mode of regulation of native in cellulo crystal formation offers a challenge to the scientists. Although the mechanism of how intracellular protein self-assembled is not known yet scientists believed that the hidden regulatory mechanism ( different from normal regulatory approach ) may have a link to a specific function which is either disease associated or new form of recombinant as a protein crystallization chamber that systematically exploit living cells.

Protein Storage

In nature, nutrient storage is observed as a normal process in living objects in the form of eggs or seeds in the form of crystallize yolk proteins as a source of  constant nutrient supply for the offspring. In the case of human eyes it was thought that the only 10 or so crystalline proteins ( like alpha (?),  beta (?) and gamma (?) ) are involved in the evolution of eyes. The remaining lens proteins are non-conserved, diverse group used as enzymes elsewhere in the body.

Sturcture of Eye Lense

Eyes collect light through an  aperture and  focus it with a lens photoreceptor cells  convert photons into neural signals. Lenses are of tightly packed proteins. n the case of human lenses (i.e. vertebrates) these are actually formed from modified epithelial cells containing highly concentrated soluble proteins, so called “crystallins” because of their packing  arrangements into an arrays ). As mentioned above that the 10 or so crystalline proteins found in human eyes which are unique to lens tissue but present thought is of the large number of crystallins i.e. alpha (?), beta (?) and gamma (?) crystallins that are indeed also specialized lens proteins. In fact, crystallins or transparent proteins are arranged in approximately 20,000 thin concentric layers (i) whose average concentration is about twice than that of other intracellular proteins, and (2) that may play a structural role during the development of eye-lens. It means that in one side the eye lens can be used as a source to study the mechanism of aggregation and deposition of other “mis-folded”  proteins that cause cataract while in another side the same eye lens provides a mechanism of aggregation of exogenous proteins whose developing approaches provides a clue how to protect the cells from the accumulation of aggregated proteins. Note that out of the earlier mentioned the 10 or so crystallins proteins alpha (?) and beta (?) crystalins are specialized lens protein  that are related to heat shock proteins (in the case of vertebrates) and schistosome  egg antigen, respectively. In case of the remaining vertebrates the lens proteins are a non-conserved and diverse group. This implies that one gene coding for a protein have two entirely different functions which is known as “gene sharing” and it may be a prelude a “gene duplication”

As mentioned earlier that in human eye (i.e. vertebrate) the alpha (?-), beta (?-) and gamma ( ?-) crystallins are known  abundant vertebrate eye lens protein because of their presence more than 90% of total proteins. Not only that, presence of enzymes  in  eye lens also act as structural proteins, receptors, connexins , water channel aquaporin and cytosketal proteins. Basically, alpha (?-) crystallin,as a small heat shock protein, interacts with partly folded proteins in a chaperone manner as wll as prevents their irreversible aggregation and precipitation,  beta (?-) and gamma ( ?-) crystallins are primarily composed of antiparallel beta (?-) sheet. Finally, these three i.e. the ?-, ?-, and ?-crystallins representing in all vertebrate lineages may have evolved from proteins that support this kind of filament system as well as may shed light on the functions of these proteins in lens and non-lens cells.

Eye lens Chaperon a-crystallins and Triaxial  shape

The a-crystallins are molecular chaperons which belongs to the small heat shock protein family. The cellular function of this ?-crystallins is to bind to partially unfolded polypeptides and nurture them  so that they are within a refolding competent state ^21-23 such that their acting as  molecular traps ultimately  protect the  cells from the consequences of irreversible protein aggregation.

There are two types ?-crystallin genes, namely, ?A and ?B . In a study of the structures of the recombinant ?-crystallins , in particular ?B-crystallins,  by electron microscope ²⁴ it was  found human ?A- and ?B- crystallins were recombinantly expressed in “ Ecscherichia Coli”. Further analysis using selected 2565 single particle images (fig.2A) and Eigenimages ( i.e. images representing the most important differences in the data set (fig.4B) and preliminary class averages (fig.2C and D) they found human  ?B-crystallin oligomer is roughly spherical with  a diameter of 13.5 nm (fig. 3A). This oligomer also accommodates a large central cavity of 8.5 nm diameter which is surrounded by a symmetrical protein shell ( with a mean thickness varying from 2.5 to 4 nm. (fig.3B). In addition, they also found the protein shell that contains

Figure 2: Observed image analysis of negatively stained ?B-crystallin Click here to view Figure

Figure 3: 3D reconstruction of human recombinant ?B-oligomers as obtained by Peschek team. 24. Click here to view Figure

openings at the positions of the 2-fold axes ( with diameter of ~ 3.5 nm ) and 3-fold axes (with 3 and 2 nm for the two unequals ). The overall structure of human recombinant ?B-crystallins is nearly circular based on the surface representation of 3D model  (fig. 3B) and density cross section through 3D  model (fig. 3B).

Aquaporin (AQP1) Water Transporter

In another investigation ²⁵  for understanding the function of protein (i.e. 28kDa ) as water transporter in human eye-lens it was demonstrated that under the injected controlled  oocyte with water in Xenopas laevis  the protein was christened “ aquaporin” ( so called “AQP1 ) such that initially with  a circular shape it deformed from its circular shape to deformed triaxial shape in the case of injected with cRNA. A noticeable change in shape they observed 30 seconds later from the time injection i.e. the AQP1 oocyte had begun swell as seen in figure 4 ( i.e. shape changes from circular to triaxial) and after 3 minutes the swelled AQP1 oocyte had further deformed ( i.e. from triaxial shape to ellipsoidal ) and finally exploded. This implies that the AQP1 oocyte changes its shape from initial circular to triaxial shape ( during the beginning of swelling) and finally exploded when triaxial shape turns into more deformed phase ( which was more unstable resulting which it exploded).

Figure 4: Shows the representation of functional expression of AQP1 water channels in Xenopus laevis oocytes observed by Preston group 25. Click here to view Figure

Results

Physical Observation of Hen-eggs

Physically observed of hen eggs by this author  are shown in figure 5. A variety of egg shapes are  circular (serial no 1), triaxial (sl. No 2,3,7), ellipsoidal (sl. No.4. 5, 6 ). Comparing the observed shape of 3D reconstruction of human recombinant ?B-crystallin with the physically observed shapes of hen’s egg it is revealed that the nearly circular shapes are triaxial shapes. This means that in human eye-lens proteins are associated in “Triaxial Shpes”. Of course, this needs further precise imaging of ?-crystallin to confirm it.

Figure 5: Physically observed hen’s egg. Clockwise (top four) — 1st is circular shape, 2nd, 3rd and (below three) 7th are in their triaxial shape while 4th , 5th, and 6th are ellipsoidal shape. Click here to view Figure

Figure 6: Comparison of the structure of protective protein in the human eye lens with the observed AQP1 and hen’s egg reveals that triaxial shape is prominent. Click here to view Figure

Discovery of  Cosmic Baby

During the analysis of  observed X-ray data (for short burst originated from magnetar) collected by  Swift X-ray telescope (XRT) Esposito team ³⁰ discovered a typical characteristic of short burst from a magnetar on 12^th March 2020 at 21:16: 49 UT ^27,28. This newly discovered magnetar was actually an uncataloged X-ray source as Swift J1818.0 – 1607and presently known as “Cosmic Baby” (see fig. 7). It is called “baby” ( with age only 240 years) in the sense that till date all the discovered magnetars are about million years aged. The significant parameters of Cosmic Baby are :

Characteristic  age    ~ 240 years ²⁹

Magnetic field strength at Surface   ~  2.7 x 10¹⁴ G

Magnetic field strength  at poles      ~ 7 x 10¹⁴ G

Spin period            = 0.7333920 s

Coherent periodicity of X-ray signal = 1.36s

Period derivative      ~ 9 x 10 ^{– 11} s.s^{-1   30}

Using the initial observed parameters at the time of discovery Parui ^{31- 33} estimated the internal core magnetic field inside the magnetar and it associated ellipticity ( a property measuring the deformation ) of this Cosmic Baby and found  8.9424 x 10¹⁷ G and 9 x 10 ^{– 3} , respectively. It is seen that the estimated deformation of this object due super-strong magnetic field turns it into a “Triaxial Star”. In fact, as its age is 240 years the estimated value hints that this cosmic baby will exhibit its triaxial nature for next 760 years. The importance of cosmic baby is that it shows the possible evidence of the existence of a “Triaxial Star” that was predicted by S. Chandrasekhar in 1969 i.e. more than 50 year ago ³⁴. This implies that physical existence of a “Triaxial Star” is possible.

Figure 7: Photographic image of Cosmic Baby i.e. Swift J1818.0 – 1607 (pink colour composited with an infrared photograph of its location in the sky ( CREDIT : Chandra X-ray Observtory, NASA ; Courtesy – Wikipedia) Click here to view Figure

Another significant finding arises from the discovery of  NANO Grav ^{35 – 37} which suggests that characteristics observed in cosmic objects , the same characteristics can also be possible to observe in human . Based on this Parui ³⁸ suggested that  triaxiality and other characteristics  possibly be observable in human.

Crystallization of Protein in  Magnetic field

Proteins play a significant role in governing almost all biochemical reactions in living things, particularly in human eye-lens from its structure formation to development. X-ray diffraction analysis shows that a protein single crystal is :

with length > 0.1 mm ;

of high quality is indispensible ;

with main problem is the crystallization that has been a bottleneck.

A possible solution to overcome these difficulties is investigation of the effect of magnetic field on protein crystallization.  In an investigation of hen-egg white lysozyme as model protein and its effect on magnetic field ³⁹ it was found that magnetic field effects on protein crystal is really a complex which needs a large quantity of high quality single protein crystal in order to understand the realistic characteristics of protein behavior, particularly on the orientation, crystal habit, growth rate of crystal, convection in aqueous solution, etc. In other words, effects of magnetic field and its magnetization force ^40,41 on protein crystal offers an opportunity to the scientists a possible clues of high-resolution structural information that ultimately leads to high quality protein crystals.

Discussion

Protein crystallization in living cells ^{42, 43}, particularly in human eye-lens plays a crucial role not only for beautiful eyes but also its various side-effects that create constraints via eye-diseases for clear vision. Investigations ^{44 – 46} of magnetic field effects on protein crystal growth provide possible clues to the scientists for obtaining high quality protein crystals that is required for clear vision’s tenure for a  long years. Discovery of Cosmic Baby hints that deformation due strong magnetic field in the form of “Triaxiality” is applicable for human eyes also . This implies that at the early birth phase of zygote formation the  human embryo may turn it’s shape into “Triaxility” when the gestational sac follow a shape change from circular to ellipsoidal. Thus, “Triaxiality” arises during the transition  from circular  to ellipsoidal shape of the gestational sac (that covers the embryo inside the  mother’s womb) provides an invaluable opportunity to the scientists for investigating the exact role of “Triaxility” for ensuring formation of beautiful eyes as well as ageless appearance in women’s body structure.

Acknowledgement

The author is greatly indebted to the anonymous reviewers for their invaluable comments and suggestions. The author wishes to thank Prof. H N K Sarma, Dept. of Physics, Manipur University, B K Ganguly, Mrs. Tapati Parui and specially to Rajarshi Parui for his help in computer works.

Funding Sources

The author(s) received no financial support for the research, authorship, and/or publication of this article

Conflict of Interest

The author does not have any conflict of interest.

Data Availability Statement

Data sharing is not applicable as no data sets were analyzed.

Ethics statement

This research did not involve human participants, animal subjects, or any material that requires ethical approval.

Informed Consent Statement

This study did not involve human.

Author contributions

I have done the complete manuscript.

References

1. Andley U P. Crystallins in the eye: Function and Pathology. Prog. Retinal & Eye Res. 2007 ; 26(1) : 78-98);
   CrossRef
2. Bhat S P, Nagineni C N. Alpha B subunit of lens-specific Protein alpha crystallin  is present om other ocular and  non-ocular tissues. Biochem. Biophys. Res. Commun. 1989 ; 158 : 329 -338
   CrossRef
3. Chayen N.E., Helliwell  J.R., Snell  E.H. : Macromolecular Crystallization and Crystal Perfection ( Oxford University  Press  : Oxford, UK . 2010).
   CrossRef
4. Park S H, Suh S W , Song H. A cytosine modification mechanism revealed by the structure of a ternary   complex of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate. IUCRJ 2019; 6 (2) : 206 - 217
   CrossRef
5. Hong B, Haddad  M, Maley F, Jensen J H, Kohen A. Hydride transfer versus hydrogen radical transfer in thymidylate synthase. J. Am. Chem Soc. 2006 ; 128 (17) : 5636 -5637
   CrossRef
6. Cai R, Yang H, He J, Zhu W. The effects of magnetic fields on water molecular hydrogen bonds.   J. Mol. Struct. 2009 ;  938 (1-3) : 15 - 19
   CrossRef
7. Chang K.-T., Weng C-I. The effect of an external magnetic field on the structure of liquid water using  molecular dynamics simulation. J. Appl. Phys. 2006 ; 100 : 043917
   CrossRef
8. Adams PD, Afonine PV, Baskaran K,  Berman H M, Berrisford  J, Bricogne G, Brown  D G, Burley S K, Chen  M, Feng  Z,  Flensburg  C,  Gutmanas A,  Hoch J C,  Ikegawa  J,  Kengaku  Y,  Krissinel   E,  Kurisu  G, Liang Y,  Liebschner  D, Mak  L ,  Markley J L,  Moriarty  N W,  Murshudov G N,  Noble  M,  Peisach E, Persikova I,  Poon  B K,  Sobolev  O V, Ulrich E L,  Velankar S,  Vonrhein C,  Westbrook J, Wojdyr M, Yokochi I M,  Young J Y. Announcing mandatory submission of pdbx/mmcif format files for crystallographicdepositions to the protein data bank (PDB). Acta Cryst. D Struct Biol.  2019 ; 75 : 451 -545
   CrossRef
9. Burley S K, Berman H M , Kleywegt G J, Markley J L , Nakamura H, Velankar S. Protein data bank (PDB) :The single global macromolecular structure archive. Methods Mol. Biol. 2017 ; 1607 : 627 - 641
   CrossRef
10. Takeda M, Miyanoiri Y, Terauchi T, Yang C J, Kainosho M. Use of h/d isotope effects to gather information about hydrogen bonding and hydrogen exchange rates. J. Magn. Reson. 2014 ; 241 (4) : 148-154
    CrossRef
11. Hodge E A, Benhaim M A, Lee K K. Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry. Protein Sci. 2020 ; 29 (4) : 843-855
    CrossRef
12. Luft J R, Wolfley J R, Said M I , Nagel R M, Lauricella A M , Smith J L , Thayer M H , Veatch C K , Snell E H , Malkowski M G , Detitta G T . Efficient optimization of crystallization conditions by manipulation of drop volume ratio and temperature. Protein Sci. 2007 ; 16 (4) : 715 - 722
    CrossRef
13. Asai T, Suzuki Y, Sazaki G, Tamura K, Sawada, T, Nakajima, K. Effects of high pressure on the solubility and growth kinetics of monoclinic lysozyme crystals. Cell. Mol. Biol. 2004 ; 50 : 329 -334
    CrossRef
14. Hammadi Z, Veesler S. New approaches on crystallization under electric fields. Prog. Biophys Mol. Biol. 2009 ; 101(1-3) : 38 - 44
    CrossRef
15. Dong J, Boggon T J, Chayen N E, Raftery J, Bi R C, Helliwell J R. Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 a resolution. Acta Cryst. D Biol. Cryst. 1999 ; 55 (Pt-4) : 745 - 752
    CrossRef
16. Pareja-Rivera C, Cuéllar-Cruz M, Esturau-Escofet N, Demitri N, Polentarutti M , Stojanoff V, Moreno A. Recent advances in the understanding of the influence of electric and magnetic fields on protein crystal growth. Cryst. Growth Des. 2016 ; 17 (1) : 135- 145
17. Hünefeld F L. Der Chemismus in der thierischen Organisation , Leipzig: Brockhaus, 1840 ; p.  158-63
18. Hartig T. Ueber das Klebermehl. Botanische Zeitung 1855 ; 13 : 881 - 882
19. Osborne T B. Crystallized vegetable proteids. Amer. Chem. J. 1892 ; 14 : 662 - 690
    CrossRef
20. Parui R K. Cosmic Baby and Crystallography — Decoding the Invisible inside the Secret of the Universe. Orient. J. Phys. Sci. 2024 ; 09 ,
21. Reichert E T, Brown A P. The Differentiation and Specifity of Corresponding Proteins and other vital substances in relation to biological classification and evolution, in The Crystallization of Hemoglobins. (Carnegie Institution, Washington, DC. 1909)
    CrossRef
22. Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 1997 ; 16 (2) : 221 - 229
    CrossRef
23. .Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem. 1993 ; 268 (3) : 1517 - 1520
    CrossRef
24. Lee G J., Roseman A.M, Saibil H.R., Vierling, E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 1997 ; 16 : 659 - 671
    CrossRef
25. Peschek J, Braun N, Franzmann T M, Buchner J. The eye lens chaperon ?-crystallin forms defined globular assemblies. PNAS. 2009 ; 106 (32) : 13272 - 13277
    CrossRef
26. Preston G M , Carroll T P, Guggino W B, Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CH1P28 Protein. Science 1992 ; 256 : 385
    CrossRef
27. Agre P. Aquaporin Water Channels , Nobel Lecture 8 December 2003 (Johns Hopkins University School of Medicine, Bultimore, MD. ) p. 184
28. Gehrels N , Chincarini G,  Giommi P,  Mason K O,  Nousek JA,  Wells AA, White  N E , Barthelmy  S D,  Burrows D N, Cominsky L R,  Hurley, K C,  Marshall FE,  Mészáros  P, Roming P W A,  Angelini  L.,  Barbier L M,  Belloni T,  Campana S,  Caraveo PA.,  Chester M M,  Citterio O,  Cline T L,  Cropper M S,  Cummings J R,  Dean A J,  Feigelson E D,  Fenimore E E,  Frail D A,  Fruchter A S,  Garmire G P.,  Gendreau K,  Ghisellini G,  Greiner J,  Hill J E, Hunsberger S D,  Krimm H A, Kulkarni S R, Kumar P, Lebrun F,  Lloyd-Ronning N.M., Markwardt C B, Mattson B J, Mushotzky R F, Norris J P,  Osborne J, Paczynski B, Palmer D M, Park H.-S, Parsons A M, Paul J, Rees J M, Reynolds C S,  Rhoads J E, Sasseen T P, Schaefer B E, Short A T,  Smale A P, Smith L A, Stella L , Tagliaferri G, Takahashi T, Tashiro M, Townsley L K, Tueller J, Turner M J L, Vietri M, Voges W, Ward  M, Willingale R, Zerbi F M, Zhang W W. The Swift Gamma Ray Bursts Mission.  Astrophys. J. 2004 ; 611 : 1005
    CrossRef
29. Gehrels N, Razzaque S. Gamma Ray Bursts in the Swift Fermi Era. Frontiers Phys. 2013 ; 8 : 661
    CrossRef
30. Evans P A, Gropp J D, Kennea J A,  Klingler  N  J, Laha  S, Lien  A Y, Page K L, Sakamoto T, Tohuvavohu, A, Neil Gehrels Swift Observatory Team. Swift BAT  trigger 960986 : Swift detection of a new  SGR Swift J 1818.0 – 1607. 2020 ; GCN Circular # 272273
31. Esposito P, Rea N,  Borghese A,  Coti Zelati F, Viganò D, Israel G L , Tiengo A, Ridolfi A, Possenti A , Burgay M, Götz D, Pintore F, Stella L, Dehman C,  Ronchi M, Campana S, Garcia-Garcia A, Graber V, Mereghetti S, Perna R,  Rodríguez Castillo G A, Turolla R,  Zane S. A very young radio-loud Magnetar.   Astrophys. J. Lett. 2020 ; 896 : L30
    CrossRef
32. Parui R K. A Remark on “Do triaxial star supermassive compact star exist ?  Int. Astron. Astrophys. Res. J. 2023 ; 5 (1) : 33-37
33. Parui R K. A New Compact Star – the “Triaxial Star” – and the Detection of a Cosmic Baby: A Possibility.   Int. Astron. Astrophys. Res. J. 2023 ; 5 (1) :  38 - 47
34. Parui R K. Cosmic Baby and detection of a new compact Star – the “Triaxial Star” : A possibility. Astrophys. Space Sci. 2023 ; 368 (6) : 46 . Revised to be submitted  (2025)
35. Chandrasekhar S. Ellipsoidal Figures of Equilibrium. (Yale Univ. Press. New Haven, USA ,1969)
36. Nano Grav Team : Agazie G, Anumarlapudi A, Archibald A M , Baker P T, Becsy B, Blecha L, Bonilla A, Brazier A, Brook P R, Burke-Spolaor S, Burnette B , Case R, Casey-Clyde J A, Charisi M, Chatterjee S, Chatziioannou K, Cheeseboro B D, Chen S, Cohen T, Cordes J M, Cornish N J , Crawford F, Cromartie H T, Crowter K, Cutler C J , D'Orazio D J, DeCesar M E, DeGan D, Demorest P B, Deng H, Dolch T, Drachler B, Ferrara E C, Fiore W , Fonseca E , Freedman G E , Gardiner E, Garver-Daniels N, Gentile P A, Gersbach KA, Glaser J, Good D C, Gültekin K, Hazboun J S, Hourihane S, Islo K, Jennings R J, Johnson A, Jones M L, Kaiser A R , Kaplan D L , Kelley L Z, Kerr M, Key J S, Laal N, Lam M T , Lamb W G, Joseph T, Lazio W, Lewandowska N , Littenberg T B , Liu T, Luo J, Lynch R S, Ma C-P, Madison D R, McEwen A, McKee M W, McLaughlin M A, McMann N, Meyers B W , Meyers P M , Mingarelli C M, Mitridate A, Natarajan P, Ng C, Nice D J, Ocker S K , Olum K D, Pennucci TT , Perera B B P, Petrov P, Pol N S , Radovan H A , Ransom S M , Ray P S, Romano J D , Runnoe J C, Sardesai S C, Schmiedekamp A, Schmiedekamp C, Schmitz K, Schult L, Shapiro-Albert B J , Siemens X, Simon J, Siwek M S, Stairs I H, Stinebring D R, Stovall K, Sun J P, Susobhanan A, Swiggum J K, Taylor J, Taylor S R, Turner J E, Unal C, Vallisneri M, Vigeland S J, Wachter J M , Wahl H M, Wang Q, Witt C A, Wright D, Young O, and The NANOGrav Collaboration.. The NANOGrav 15 yr Data set : Constraints on Supermassive Black hole Binaries from the gravitational wave background. Astrophys. J. Lett. 2023 ; 952 : L37
    CrossRef
37. Nano Grav. Team. Agazie G, Anumarlapudi A, Archibald A M, Baker P T, B. Becsy, B. Blecha, Blecha L, Brazier A, Brook P R, Burke-Spolaor S, Burnette R, Case R, Charisi M, Chatterjee S, Chatziioannou K, Cheeseboro B D, Chen S, Cohen T, Cordes J M, Cornish N J , Crawford F, Cromartie H T , Crowter K, Cutler C J, DeCesar M E, DeGan D, Demorest P B, Deng H, Dolch T, Drachler B, Ellis J A, Ferrara E C , Fiore W, Fonseca E, Freedman G E, Garver-Daniels N, Gentile P A,Gersbach K A, Glaser J, Good D C, Gultekin K, Hazboun J S, Hourihane S, Islo K, Jennings R J, Johnson, A D, Jones M L, Kaiser A R, Kaplan D L, Kelley L Z, Kerr M, Key J S, Klein T C, Laal C, Lam M T, Lamb W G, Joseph T, Lazio W, Lewandowska N, Littenberg T B, Liu T, Lommen A, Lorimer D R, Luo J, Lynch R S, Ma C-P, Madison D R, Mattson M A, McEwen A , McKee J A, McLaughlin M A, McMann N, Meyers B W, Meyers, P M, Mingarelli C, Mitridate A, Natarajan, Ng C, Nice D J, Ocker S K, Olum K D , Pennucci T T , Perera B B P, Petrov P, Pol N S, Radovan H A, Ransom S M, Ray P S , Romano J D , Sardesai S C, Schmiedekamp A, Schmiedekamp C, Schmitz K, Schult L, Shapiro-Albert B J , Siemens X, Simon J, Siwek M S , Stairs I H , Stinebring D R , Stovall K , Sun J P, Susobhanan A, Swiggum J K , Taylor J, Taylor S R , Turner J E, Unal C, Vallisneri M, van Haasteren R, Vigeland S J, Wahl H M , Wang Q, Witt C A , Young O. The NANOGrav 15 yr Data Set: Evidence for a Gravitational-wave Background . Astrophys. J. Lett. 2023 ; 951: L8
    CrossRef
38. Nano Grav Team : Agazie G, Alam M F , Anumarlapudi A, Archibald AM , Arzoumanian Z, Baker P T, Blecha L , Bonidie V, Brazier A, Brook P R , Burke-Spolaor S, Bécsy B, Chapman C, Charisi M, Chatterjee S, Cohen T, Cordes J M, Cornish N J , Crawford F , Cromartie H T, Crowter K , DeCesar M E , Demorest P B , Dolch T , Drachler B, Ferrara E C, Fiore W, Fonseca E , Freedman G E , Garver-Daniels N, Gentile P A , Glaser J, Good D C , Gültekin K , Hazboun J S , Jennings R J, Jessup C, Johnson A D, Jones M L , Kaiser A R , Kaplan D L , Kelley K Z , Kerr M, Key J S , Kuske A, Laal N, Lam M T , Lamb W J , Lazio T J W, Lewandowska N, Lin Y, Liu T, Lorimer D R , Luo J, Lynch R S, Ma C P , Madison D R , Maraccini K , McEwen A, McKee J W , McLaughlin M A , McMann N, Meyers B W, Mingarelli C M F, Mitridate A, Ng C, Nice D J , Ocker S K , Olum K D , Panciu E , Pennucci T T , Perera B B P , Pol N S , Radovan H A , Ransom S M , Ray P S , Romano J D , Salo L, . Sardesai S C , Schmiedekamp C, Schmiedekamp A, Schmitz K, Shapiro-Albert B J , Siemens X, Simon J, Siwek M S , Stairs I H , Stinebring D R, Stovall K , Susobhanan A, Swiggum J K , Taylor S R , Turner J E , Unal C, Vallisneri M, Vigeland J, Wahl H M, Wang Q, Witt C A , Young O, and The NANOGrav Collaboration. The NANOGrav 15 yr Data Set: Observations and Timing of 68 Millisecond Pulsars. Astrophys. J. Lett. 2023 ; 951 : L9
    CrossRef
39. Parui R K. Cosmic Baby and Human Baby — Do both of them exhibit a similar type characteristics as cosmic connection to human ? : A possibility . Revised version submitted to Euro. Phys. J. C (2024)
40. Sazaki G, Yanagiya S, Durbin S D, Miyashita S , Nakada T, Komatsu H, Ujihara T, Nakajima K, Watanabe K , Motokawa M. Effects of a Magnetic field on the Crystallization of Protein. in Materials Science in Static High Magnetic fields, eds: M Motokawa , K. Watanabe . Springer-Verlag, Berlin Heidelberg. 2002 , p. 283
    CrossRef
41. Alka M, Wakayama N I. Effects of a magnetic field and magnetization force on Protein crystal growth: Why does a magnet improve the quality of some crystals ? Acta Cryst. D 2002 ; 58 : 1708 - 1710
    CrossRef
42. Alka M. The influence of magnetic field on protein crystal growth and quality. Deutsches Elektronen Synchrotron (DESY), Hamburg, Germany (2005)
43. Schonherr R, Rudolph J M, Redecke L. Protein crystallization in Living Cells. Biol. Chem. 2018 ; 339 (7) : 751- 772
    CrossRef
44. Jiang M, Zhang L, Wang F, Zhang J, Liu G, Gao B, Wei D. Novel application of Magnetic protein: Convenient one-step purification and immobilization of proteins. Nature (Scientific Reports) 2017 ; 7 (1) : 13329 -13329
    CrossRef
45. Ryu S Y, Oh I H, Cho S J, Shin A K, Hyun K S. Enhancing protein crystallization under a Magnetif field, Crystals 2020 ; 10 (9) : 821
    CrossRef
46. Schey K L, Wang Z, Wenke J L, Ai Y . Aquaporins in the eye: Expression, function, and roles in Ocular disease. Biochim. Biophys. Acta. 2014 ; 1840 : 1513 - 1523
    CrossRef
47. Surade S, Ochi T, Nietlispach D, Chirgadze D , Moreno A. Investigation into Protein Crystallization in the presence of a strong magnetic field. Crystal. Growth. Design. 2010 ; 10 : 691- 699
    CrossRef