THE RELATION BETWEEN STRUCTURE AND FUNCTION IN HEMOGLOBINS

1964 ◽  
Vol 42 (6) ◽  
pp. 763-775 ◽  
Author(s):  
Austen Riggs

Many lines of evidence indicate that the oxygenation of hemoglobin is accompanied by changes in protein structure. Data on the oxygen equilibria of the hemoglobins from a number of animals are discussed in terms of this evidence. Evidence from studies of some hemoglobins (lamprey, frog and tadpole) indicates a major role for subunit dissociation equilibria in explaining two properties of the oxygen equilibria: heme–heme interaction and the "Bohr effect". The importance of subunit dissociation in mammalian hemoglobins is suggested by the known concentration dependence of the oxygen equilibria. Mammalian hemoglobins are composed of two types of polypeptide chains, α and β. The idea that the α and β subunits have different oxygen equilibria and are affected differently by pH is examined. It is concluded that the β-chains appear to play a major role in the mechanism of the Bohr effect not shared by the α-chains. This conclusion is supported by the structural changes in hemoglobin found to occur upon oxygenation by X-ray diffraction techniques.

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Alexey Rozov ◽  
Iskander Khusainov ◽  
Kamel El Omari ◽  
Ramona Duman ◽  
Vitaliy Mykhaylyk ◽  
...  

1973 ◽  
Vol 6 (2) ◽  
pp. 139-199 ◽  
Author(s):  
Rudolf Rigler ◽  
Måns Ehrenberg

Spectroscopic probes have become powerful tools in analysing the correlation between structure and function of biological macromolecules. Though these spectral methods cannot give as circumstantial information about the anatomy of a biological structure as, for example, X-ray diffraction they can provide information on physical properties at defined loci in a macromolecule which are not accessible by other techniques. Most important, spectroscopic studies have provided means to study the dynamics of structural changes and interactions in time domains spanning from nanoseconds and less up to infinite time.


2018 ◽  
Vol 879 ◽  
pp. 108-112 ◽  
Author(s):  
Nisakorn Nuamsrinuan ◽  
Pichet Limsuwan ◽  
Kittisakchai Naemchanthara

In this paper, the cockle shell was studied as a catalyzer for biodiesel production. The cockle shell was heated at the various temperatures from 200 to 1300 °C for 4 h in the furnace. Then, the crystal structure and function group of unheated and heated cockle shell were characterized by X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR), respectively. The results indicated that the initial phase of cockle shell is aragonite phase. After heat at 400 °C, the aragonite phase transformed to calcite phase. Moreover, the calcite phase of cockle shell was completely changed to calcium oxide (CaO) after heated at 800 °C. Eventually, the yield of biodiesel used the CaO derived from cockle shell were determined by nuclear magnetic resonance spectroscopy (NMR). The results show that the CaO derived from cockle shell can be used as a catalyzer of biodiesel preparation. However, the biodiesel used CaO from cockle shell after heated at 1100 to 1300 °C as a catalyzer have the higher yield than other heated temperature. Finally, the results of this research indicated that the CaO from cockle shell could be used as a catalyst for biodiesel production.


Author(s):  
William H. Massover

Molecules of the metalloprotein, ferritin, have an outer shell comprised of a polymeric assembly of 24 polypeptide subunits (apoferritin). This protein shell encloses a hydrated space, the central cavity, within which up to several thousand iron atoms can be deposited as the biomineral, ferrihydrite. The actual pathway taken by iron moving across the protein shell is not known; an analogous question exists for the demonstrated entrance of negative stains into the central cavity. Intersubunit interstices at the 4-fold and 3-fold symmetry axes have been defined with x-ray diffraction, and were hypothesized to provide a pathway for penetration through the outer shell; however, since these channels are only 4Å in width, they are much too small to allow simple permeation of either hydrated iron or stain ions. A different hypothesis, based on studies of subunit dissociation from highly diluted ferritin, proposes that transient gaps in the protein shell are created by a rapid reversible subunit release and permit the direct passage of large ions into the central cavity.


1999 ◽  
Vol 82 (08) ◽  
pp. 271-276 ◽  
Author(s):  
Glen Spraggon ◽  
Stephen Everse ◽  
Russell Doolittle

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide


2014 ◽  
Vol 70 (a1) ◽  
pp. C94-C94
Author(s):  
Pawel Kuczera ◽  
Walter Steurer

The structure of d(ecagonal)-Al-Cu-Rh has been studied as a function of temperature by in-situ single-crystal X-ray diffraction in order to contribute to the discussion on energy or entropy stabilization of quasicrystals (QC) [1]. The experiments were performed at 293 K, 1223 K, 1153 K, 1083 K, and 1013 K. A common subset of 1460 unique reflections was used for the comparative structure refinements at each temperature. The results obtained for the HT structure refinements of d-Al-Cu-Rh QC seem to contradict a pure phasonic-entropy-based stabilization mechanism [2] for this QC. The trends observed for the ln func(I(T1 )/I(T2 )) vs.|k⊥ |^2 plots indicate that the best on-average quasiperiodic order exists between 1083 K and 1153 K, however, what that actually means is unclear. It could indicate towards a small phasonic contribution to entropy, but such contribution is not seen in the structure refinements. A rough estimation of the hypothetic phason instability temperature shows that it would be kinetically inaccessible and thus the phase transition to a 12 Å low T structure (at ~800 K) is most likely not phason-driven. Except for the obvious increase in the amplitude of the thermal motion, no other significant structural changes, in particular no sources of additional phason-related configurational entropy, were found. All structures are refined to very similar R-values, which proves that the quality of the refinement at each temperature is the same. This suggests, that concerning the stability factors, some QCs could be similar to other HT complex intermetallic phases. The experimental results clearly show that at least the ~4 Å structure of d-Al-Cu-Rh is a HT phase therefore entropy plays an important role in its stabilisation mechanism lowering the free energy. However, the main source of this entropy is probably not related to phason flips, but rather to lattice vibrations, occupational disorder unrelated to phason flips like split positions along the periodic axis.


2003 ◽  
Vol 802 ◽  
Author(s):  
R. G. Haire ◽  
S. Heathman ◽  
T. Le Bihan ◽  
A. Lindbaum ◽  
M. Iridi

ABSTRACTOne effect of pressure on elements and compounds is to decease their interatomic distances, which can bring about dramatic perturbations in their electronic nature and bonding, which can be reflected in changes in physical and/or chemical properties. One important issue in the actinide series of elements is the effect of pressure on the 5f-electrons. We have probed changes in electronic behavior with pressure by monitoring structure by X-ray diffraction, and have studied several actinide metals and compounds from thorium through einsteinium. These studies have employed angle dispersive diffraction using synchrotron radiation, and energy dispersive techniques via conventional X-ray sources. The 5f-electrons of actinide metals and their alloys are often affected significantly by pressure, while with compounds, the structural changes are often not linked to the involvement of 5 f-electron. We shall present some of our more recent findings from studies of selected actinide metals, alloys and compounds under pressure. A discussion of the results in terms of the changes in electronic configurations and bonding with regard to the element's position in the series is also addressed.


2005 ◽  
Vol 38 (5) ◽  
pp. 749-756 ◽  
Author(s):  
Ulrich Gesenhues

The polygonization of 200 nm rutile crystals during dry ball-milling at 10gwas monitored in detail by means of transmission electron microscopy (TEM) and X-ray diffraction (XRD). The TEM results showed how to modify the Williamson–Hall method for a successful evaluation of crystal size and microstrain from XRD profiles. Macrostrain development was determined from the minute shift of the most intense reflection. In addition, changes in pycnometrical density were monitored. Accordingly, the primary crystal is disintegrated during milling into a mosaic of 12–35 nm pieces where the grain boundaries induce up to 1.2% microstrain in a lower layer of 6 nm thickness. Macrostrain in the interior of the crystals rises to 0.03%. The pycnometrical density, reflecting the packing density of atoms in the grain boundary, decreases steadily by 1.1%. The results bear relevance to our understanding of plastic flow and the mechanism of phase transitions of metal oxides during high-energy milling.


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