Christo N. Nanev

ORCID: 0000-0003-0678-737X
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About
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Research Areas
  • Crystallization and Solubility Studies
  • Enzyme Structure and Function
  • nanoparticles nucleation surface interactions
  • Protein Structure and Dynamics
  • Solidification and crystal growth phenomena
  • Freezing and Crystallization Processes
  • Protein purification and stability
  • Crystallography and molecular interactions
  • Force Microscopy Techniques and Applications
  • Proteins in Food Systems
  • Advanced Surface Polishing Techniques
  • Pickering emulsions and particle stabilization
  • Chemical Thermodynamics and Molecular Structure
  • Spectroscopy and Quantum Chemical Studies
  • Electrodeposition and Electroless Coatings
  • Corrosion Behavior and Inhibition
  • Surface Chemistry and Catalysis
  • Biochemical Acid Research Studies
  • Advanced Electron Microscopy Techniques and Applications
  • X-ray Diffraction in Crystallography
  • Surface Roughness and Optical Measurements
  • Advanced X-ray Imaging Techniques
  • Physiological and biochemical adaptations
  • Nanoparticle-Based Drug Delivery
  • Aquatic and Environmental Studies

Institute of Physical Chemistry
2014-2025

Bulgarian Academy of Sciences
2014-2023

Universidad Nacional Autónoma de México
2019

University of Massachusetts Amherst
2019

University of St Andrews
2019

Soongsil University
2019

Jichi Medical University
2019

Tohoku University
2019

Lodz University of Technology
2019

Institute of Physics
2019

The most powerful method for protein structure determination is X-ray crystallography which relies on the availability of high quality crystals. Obtaining crystals a major bottleneck, and inducing their nucleation crucial importance in this field. An effective to form introduce nucleation-inducing heterologous materials into crystallization solution. Porous are exceptionally at nucleation. It shown here that combined diffusion-adsorption effect can increase concentration inside pores,...

10.1038/srep35821 article EN cc-by Scientific Reports 2017-01-16

The rate of nucleation crystals is the subject extensive research, since it—together with time—determines number growing; in turn, their related to size. Experimental studies show that, for biomolecular crystals, despite required unusually high supersaturations, process distinctly slow. This slowness arises from inherent peculiarity such crystals. Therefore, a prerequisite management crystallization towards desired outcome molecular level understanding mechanism. In this paper, analyzing...

10.3390/cryst15040332 article EN cc-by Crystals 2025-03-31

Number density of insulin crystals versus nucleation time dependences were measured simultaneously, during the same experiment, at four typical places: in solution bulk, glass support, air/solution interface, and solution/glass/air boundary. Stationary rates determined from linear parts corresponding plots, energy barriers for nucleus formation sizes estimated. A key finding present investigation was that, surprisingly, lowest barrier (3.8 × 10−13 erg), correspondingly smallest size (six...

10.1021/cg1011499 article EN Crystal Growth & Design 2010-11-17

10.1016/j.jcrysgro.2015.07.007 article EN publisher-specific-oa Journal of Crystal Growth 2015-07-15

Although they require surprisingly high supersaturations, both nucleation and growth of protein crystals proceed substantially more slowly as compared to small molecule crystallization. The slow the is explained by steric restriction for association molecules that due their highly inhomogeneous surfaces. Over surfaces, proteins exhibit a limited number discrete patches are only attractive portions on molecule. A simple model crystal has been devised this basis, which enables calculations...

10.1021/cg0780807 article EN Crystal Growth & Design 2007-06-26

Three-dimensional protein molecule structures are essential for acquiring a deeper insight of the human genome, and developing novel protein-based pharmaceuticals. X-ray diffraction studies such require well-diffracting crystals. A set external physical factors may promote direct crystallization so that crystals obtained useful studies. Application electric fields aids control over crystal size quality. Protein nucleation growth in presence reviewed. notion mesoscopic level impact on...

10.3390/cryst7100310 article EN cc-by Crystals 2017-10-15

Abstract The nucleation of protein crystals is reconsidered taking into account the specificity molecules. In contrast to homogeneous surface properties small molecules, molecule highly inhomogeneous. Over their surfaces proteins exhibit high anisotropic distribution patches, which are able form crystalline bonds, crystallization patch representing only a fraction total molecule. Therefore, an appropriate spatial orientation colliding molecules required in order create cluster. This scenario...

10.1002/crat.200610761 article EN Crystal Research and Technology 2006-12-22

10.1016/j.pcrysgrow.2013.09.001 article EN Progress in Crystal Growth and Characterization of Materials 2013-10-26

Macromolecular crystallization is crucial to a large number of scientific fields, including structural biology; drug design, formulation, and delivery; manufacture biomaterials; preparation foodstuffs. The purpose this study facilitate control crystallization, by investigating hydrophobic interface-assisted protein both theoretically experimentally. application liquids as nucleation promoters or suppressors has rarely been investigated, provides an underused avenue explore in...

10.1021/acsami.8b20995 article EN ACS Applied Materials & Interfaces 2019-03-12

Abstract Nucleation of protein crystals by gold nanoparticles was observed. Lysozyme and ferritin were used as model proteins. The effect established with uncoated coated 16‐mercaptodecanoic acid. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

10.1002/crat.200811125 article EN Crystal Research and Technology 2008-03-28

The heterogeneous nucleation of hen-egg-white lysozyme (HEWL) crystals has been repeatedly investigated using a double-(thermal)-pulse technique, thus detaching from growth stage. n(t) dependencies the nucleus number n, on templates poly-L-lysine, vs time, t were plotted and steady-state rates I determined. They compared with results obtained earlier for surfaces rendered hydrophobic (by means hexamethyl-disilazane) as well bare glass surfaces. In present paper we determine HEWL molecules in...

10.1002/(sici)1521-4079(200002)35:2<189::aid-crat189>3.0.co;2-u article EN Crystal Research and Technology 2000-02-01

10.1016/s0960-8974(97)00023-5 article EN Progress in Crystal Growth and Characterization of Materials 1997-01-01

Abstract Heterogeneous (on‐glass) protein crystal nucleation was separated from the bulk one in systems of thin solution layers, confined between two glass plates custom made quasi two‐dimensional all‐glass cells, as well by applying forced flow. Two commercial samples hen‐egg‐white lysozyme, Seikagaku and Sigma were used model proteins. Applying classical technique separation time growth stages with layers thickness 0.05 cm we found that on‐glass prevailed highly HEWL, while on opposite,...

10.1002/crat.200900645 article EN Crystal Research and Technology 2010-01-18

10.1016/s0927-7757(02)00175-9 article EN Colloids and Surfaces A Physicochemical and Engineering Aspects 2002-09-01

The nucleation of horse spleen ferritin (HSF) crystals on substrates was investigated using a new modification the double pulse technique. influence three different structureless * (glass, glass covered by methyl groups and poly-L-lysin template) studied. boundaries in phase-diagram, which separate zones crystal growth were obtained keeping pH = 5.0, CdSO 4 as crystallizing agent. steady-state rates determined. energy required for critical nuclei formation evaluated (10 -13 erg) sizes found...

10.1107/s0907444902014452 article EN Acta Crystallographica Section D Biological Crystallography 2002-09-26
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