Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “stability”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 199 records · Page 11Linked to original sources
PubMed2002

Stability and nickel binding properties of peptides designed as scaffolds for the stabilization of Ni(II)-Fe(4)S(4) bridged assemblies.

Helix-loop-helix peptides containing 63 residues (HC(4)H(2), HC(4)HC, HC(5)H), designated by their sequence and content of histidyl (H) and cysteinyl (C) residues, have been previously synthesized for the purpose of stabilizing certain bridged metal sites in proteins. These peptides bind one Fe(4)S(4) cluster by means of a ferredoxin tricysteinyl consensus sequence and an additional Cys residue, and one Ni(II) atom (HC(4)H(2), HC(5)H) in predesigned binding sites. In this investigation, the apopeptides and their Fe(4)S(4) derivatives are shown to be relatively stable to unfolding by guanidine hydrochloride, indicating stability of secondary structure. With this property demonstrated, Ni(II) binding equilibria have been evaluated in the terms of site-specific (Scatchard model) and stepwise (stoichiometric) binding constants. Two peptides were designed to have preformed CysHis(3) (HC(4)H(2)) and Cys(2)His(2) (HC(5)H) binding sites. The data indicate one strong binding site in each peptide with preferred binding constants k(1)=4.4x10(5) M(-1)(HC(4)H(2)) and 2.7x10(5) M(-1)(HC(5)H). Based on X-ray absorption spectroscopic data, these binding steps are associated with the formation of the desired coordination units Ni(II)CysHis(3) and Ni(II)Cys(2)His(2). For peptide HC(4)HC, k(1)=2.5x10(5) M(-1), but the binding site could not be fully identified. Collective evidence from this and prior investigations supports the presence of the bridged assemblies Ni(II)-(mu(2)-S x Cys)-[Fe(4)S(4)], stabilized by a scaffolding effect in peptides HC(4)H(2) and HC(5)H. The assembly Ni(II)-X-[Fe(4)S(4)] is the minimal structure of the A-Cluster of carbon monoxide dehydrogenase adduced from spectroscopic evidence; bridge X is currently unidentified. These results suggest that de novo designed peptides may serve as scaffolds for the construction of native bridged sites in proteins. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0320-4.

Amino Acid Sequence↗
PubMed1986

Fluorescence polarization studies on Escherichia coli membrane stability and its relation to the resistance of the cell to freeze-thawing. II. Stabilization of the membranes by polyamines.

The effects of polyamines, spermine, spermidine and putrescine on the stabilization of the membrane organization of Escherichia coli cells were studied using measurements of fluorescence polarization change of extrinsic fluorescence probes in membrane specimens as a function of temperature. The effects of the polyamines on the restoration of the cell viability after freeze-thawing were also investigated. In logarithmic-phase membrane specimens, polyamines depressed the polarization ratio increase below the transition temperatures in a dose-dependent manner. The physiologically relevant concentration of polyamines repressed the ratios to the same levels as are obtained with the stationary-phase specimens. In the stationary-phase specimens, no effect of polyamines on repression of the polarization increase was observed. A preliminary exposure of logarithmic-phase cells to polyamines protected the cells from the reduction of viability in freeze-thawing. However, a considerably high concentration and a certain length of preincubation time were required in order to an effect to be exerted. These results indicate that the intracellular polyamines could stabilize the membrane organization of logarithmic-phase cells to the same extent as in the stationary-phase cell membranes. It is conjectured that the membrane stability which is mediated by the polyamines results in cellular resistance to freeze-thawing, as it is attained by increasing the growth phase of the cells.

Cell Membrane↗
PubMed1985

The stability of bacteriophage T4 gene 32 mRNA: a 5' leader sequence that can stabilize mRNA transcripts.

In T4-infected cells, the gene 32 monocistronic mRNA is very stable. To study the molecular basis for this stability, we have constructed chimeric plasmids containing the monocistronic promoter and the gene 32 translation initiation sequence fused to either most of the E. coli lac operon or only a segment of the lacZ gene, followed by the gene 32 transcription terminator. The resulting hybrid transcripts are unstable in uninfected cells. In phage-infected cells, however, the hybrid mRNAs are at least as stable as gene 32 mRNA itself. Analysis of other plasmid constructs indicates that the sequences on the gene 32 mRNA from its 5' end to slightly beyond the initiation codon suffice to stabilize these hybrids. Studies with a series of deletions of the gene 32 leader sequence suggest that an RNA sequence near the gene 32 initiation codon is involved. Various models to explain this mRNA stabilization are discussed.

DNA Helicases↗
PubMed2004

The skeletal stability of one-piece Le Fort 1 osteotomy to advance the maxilla; Part 1. Stability resulting from non-bone grafted rigid fixation.

During the past decade, we have increasingly preferred to do a one-piece Le Fort 1 osteotomy to advance the maxilla, sometimes in isolation to treat patients with maxillary retrusive skeletal Class III patients or combined with mandibular advancement to treat bimaxillary retrusive skeletal Class II. Clinical impressions of rigid fixation techniques have indicated that there is improved stability when compared with wire fixation. There are few studies in the literature that have addressed relapse following one-piece Le Fort 1 osteotomy to advance the maxilla. Such surgery involves one single spatial movement and thereby eliminates other possible surgical variables, which may impact on the degree of stability achievable postoperatively. We studied 45 patients who had undergone a uniform one-piece maxillary advancement with elimination of controllable variables, apart from 15 patients who had simultaneous mandibular advancement. Rigid fixation was adopted throughout the study. The mean surgical change documented was 7.42 mm. The mean stability calculated at 12 months revealed a relapse of 0.72 mm (10%). This was not significant (P = 0.3). We conclude that the Le Fort 1 advancement osteotomy is a stable and surgically predictable procedure that gives only slight relapse at 12 months.

Adolescent↗
PubMed2006

Drug permeability across a phospholipid vesicle-based barrier 2. Characterization of barrier structure, storage stability and stability towards pH changes.

Recently we reported on the development of a phospholipid vesicle-based barrier as a medium throughput method for screening of drug permeability. The aim of this present study is to characterize the barrier structure, including an estimation of the amount of phospholipid within it, its storage stability and its stability over various pH ranges found in different parts of the gastrointestinal tract. The amount of lipid in the barrier was quantified using a colorimetric phospholipase D-based assay. The total amount averaged 3.30mg phospholipid per barrier. The preparation process comprises the consecutive deposition of two types of liposomes on a filter support. We estimated that the smallest liposomes, with a mean diameter of 298nm, would fill the pore volume of the filter when tightly packed. The volume of the bigger liposomes, deposited on top of the filter, was calculated to generate a 0.1mm thick layer. Visualisation of fluorescently labelled liposomes by confocal laser-scanning microscopy confirmed that the pores of the filter were completely filled with liposomes and that there was a liposome layer on top. Small angle X-ray scattering (SAXS) analysis was used to study the lamellarity of the liposomes. The liposomes contained oligo- and/or multilamellar structures before and after deposition. The functionality of the barriers during storage at three different temperatures was examined for a period of up to 4 weeks by measuring the permeability of the hydrophilic marker calcein across them. The conclusion was that the phospholipid vesicle-based barriers could be stored at -80 degrees Celsius for up to 2 weeks without significant changes. The stability of the barriers in a pH range from 2.0 to 8.0 was investigated by performing permeation studies with fluorescein at different pH values. It was found that the phospholipid vesicle-based barrier did not lose its integrity within this range. Thus, the barriers appear suitable for further studies to provide insight into segmental absorption in the human gastrointestinal tract. Furthermore, because the phospholipid vesicle-based barrier can be stored, larger batches can be produced. This makes the phospholipid vesicle-based barrier more appropriate for high throughput screening.

Crystallography, X-Ray↗
PubMed2004

Stability and demulsification of emulsions stabilized by asphaltenes or resins.

Experimental data are presented to show the influence of asphaltenes and resins on the stability and demulsification of emulsions. It was found that emulsion stability was related to the concentrations of the asphaltene and resin in the crude oil, and the state of dispersion of the asphaltenes and resins (molecular vs colloidal) was critical to the strength or rigidity of interfacial films and hence to the stability of the emulsions. Based on this research, a possible emulsion minimization approach in refineries, which can be implemented utilizing microwave radiation, is also suggested. Comparing with conventional heating, microwave radiation can enhance the demulsification rate by an order of magnitude. The demulsification efficiency reaches 100% in a very short time under microwave radiation.

Journal Article↗
PubMed2006

Tandem dimerization of the human p53 tetramerization domain stabilizes a primary dimer intermediate and dramatically enhances its oligomeric stability.

Tetramerization of the human p53 tumor suppressor protein is required for its biological functions. However, cellular levels of p53 indicate that it exists predominantly in a monomeric state. Since the oligomerization of p53 involves the rate-limiting formation of a primary dimer intermediate, we engineered a covalently linked pair of human p53 tetramerization (p53tet) domains to generate a tandem dimer (p53tetTD) that minimizes the energetic requirements for forming the primary dimer. We demonstrate that p53tetTD self-assembles into an oligomeric structure equivalent to the wild-type p53tet tetramer and exhibits dramatically enhanced oligomeric stability. Specifically, the p53tetTD dimer exhibits an unfolding/dissociation equilibrium constant of 26 fM at 37 degrees C, or a million-fold increase in stability relative to the wild-type p53tet tetramer, and resists subunit exchange with monomeric p53tet. In addition, whereas the wild-type p53tet tetramer undergoes coupled (i.e. two-state) dissociation/unfolding to unfolded monomers, the p53tetTD dimer denatures via an intermediate that is detectable by differential scanning calorimetry but not CD spectroscopy, consistent with a folded p53tetTD monomer that is equivalent to the p53tet primary dimer. Given its oligomeric stability and resistance against hetero-oligomerization, dimerization of p53 constructs incorporating the tetramerization domain may yield functional constructs that may resist exchange with wild-type or mutant forms of p53.

Calorimetry, Differential Scanning↗
PubMed2003

Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex.

Max is a member of the b-HLH-LZ (basic region-helix1-loop-helix2-leucine zipper) family of eukaryotic transcription factors. It is the obligate partner of the related b-HLH-LZ proteins, c-Myc and Mad1, with which it forms heterodimers on target DNA. While c-Myc and Mad1 require Max for DNA-binding, Max itself can form a homodimer that recognizes E-box DNA sequences (CACGTG) in gene promoters that are targeted by c-Myc. Evidence suggests that this mode of binding by Max may repress c-Myc transcriptional activity, and this may have applications in the control of the aberrant activity of c-Myc during certain oncogenic transformations. To enhance this repressive potential of Max, we sought to stabilize Max homodimers. We have designed a double mutant (N78V/H81L) located in the coiled-coil interface of the leucine zipper domain and we demonstrate that these mutations do indeed increase the stability of the protein. The mutations also improve the stability of the complex with cognate DNA. Thermal denaturations monitored by circular dichroism reveal two transitions that are due to intermediate folding states for both the wild-type and mutant proteins; this is supported by detailed thermodynamic analyses. A formalism to characterize the temperature-dependence of the unfolding, including the effect of intermediates, is presented.

Amino Acid Sequence↗
PubMed2001

Mood stabilizers regulate cytoprotective and mRNA-binding proteins in the brain: long-term effects on cell survival and transcript stability.

Manic depressive illness (MDI) is a common, severe, chronic and often life-threatening illness. Despite well-established genetic diatheses and extensive research, the biochemical abnormalities underlying the predisposition to, and the pathophysiology of, these disorders remain to be clearly established. Despite formidable obstacles in our attempts to understand the underlying neurobiology of this illness, there is currently considerable excitement about the progress that is being made using novel strategies to identify changes in gene expression that may have therapeutic relevance in the long-term treatment of MDI. In this paper, we describe our recent research endeavours utilizing newer technologies, including a concerted series of mRNA RT-PCR studies, which has led to the identification of novel, hitherto completely unexpected targets for the long-term actions of mood stabilizers - the major cytoprotective protein bcl-2, a human mRNA binding (and stabilizing) protein, AUH, and a Rho kinase. These results add to the growing body of data suggesting that mood stabilizers may bring about some of their long-term benefits by enhancing neuroplasticity and cellular resilience. These results are noteworthy since recent morphometric brain imaging and post-mortem studies have demonstrated that MDI is associated with the atrophy and/or loss of neurons and glia. The development of novel treatments which more directly target molecules involved in critical CNS cell survival and cell death pathways have the potential to enhance neuroplasticity and cellular resilience, and thereby modulate the long-term course and trajectory of these devastating illnesses.

Animals↗
PubMed1992

Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains on CPa-1 which are shielded from N-hydroxysuccinimide biotinylation by the manganese-stabilizing protein.

The structural organization of photosystem II proteins has been investigated by use of the amino group-labeling reagent N-hydroxysuccinimidobiotin (NHS-biotin) and calcium chloride-washed photosystem II membranes. We have previously shown that the presence of the extrinsic, manganese-stabilizing protein on photosystem II membranes prevents the modification of lysyl residues located on the chlorophyll protein CPa-1 (CP-47) by NHS-biotin [Bricker, T. M., Odom, W. R., & Queirolo, C. B. (1988) FEBS Lett. 231, 111-117]. Upon removal of the manganese-stabilizing protein by calcium chloride-washing, CPa-1 can be specifically modified by treatment with NHS-biotin. Preparative quantities of biotinylated CPa-1 were subjected to chemical cleavage with cyanogen bromide. Two major biotinylated peptides were identified with apparent molecular masses of 11.8 and 15.7 kDa. N-terminal sequence analysis of these peptides indicated that the 11.8-kDa peptide was 232G-330M and that the 15.7-kDa peptide was 360P-508V. The 15.7-kDa CNBr peptide was subjected to limited tryptic digestion. The two smallest tryptic fragments identified migrated at apparent molecular masses of 9.1 (nonbiotinylated) and 7.5 kDa (biotinylated). N-terminal sequence analysis and examination of the predicted amino acid sequences of these peptides suggest that the 9.1-kDa fragment was 422R-508V and that the 7.5-kDa fragment was 360P-421A. These results strongly suggest that two NHS-biotinylated domains, 304K-321K and 389K-419K, become exposed on CPa-1 when the manganese-stabilizing protein is removed by CaCl2 treatment. Both of these domains lie in the large extrinsic loop E of CPa-1.

Amino Acid Sequence↗
PubMed1999

Min-21 and min-23, the smallest peptides that fold like a cystine-stabilized beta-sheet motif: design, solution structure, and thermal stability.

Small disulfide-rich proteins provide examples of simple and stable scaffolds for design purposes. The cystine-stabilized beta-sheet (CSB) motif is one such elementary structural motif and is found in many protein families with no evolutionary relationships. In this paper, we present NMR structural studies and stability measurements of two short peptides of 21 and 23 residues that correspond to the isolated CSB motif taken from a 28-residue squash trypsin inhibitor. The two peptides contain two disulfide bridges instead of three for the parent protein, but were shown to fold in a native-like fashion, indicating that the CSB motif can be considered an autonomous folding unit. The 23-residue peptide was truncated at the N-terminus. It has a well-defined conformation close to that of the parent squash inhibitor, and although less stable than the native protein, it still exhibits a high T(m) of about 100 degrees C. We suggest that this peptide is a very good starting building block for engineering new bioactive molecules by grafting different active or recognition sites onto it. The 21-residue peptide was further shortened by removing two residues in the loop connecting the second and third cysteines. This peptide exhibited a less well-defined conformation and is less stable by about 1 kcal mol(-)(1), but it might be useful if a higher flexibility is desired. The lower stability of the 21-residue peptide is supposed to result from inadequate lengths of segments connecting the first three cysteines, thus providing new insights into the structural determinants of the CSB motif.

Amino Acid Sequence↗
PubMed2000

Preparation, X-ray crystal structure determination, lattice potential energy, and energetics of formation of the salt S4(AsF6)2.AsF3 containing the lattice-stabilized tetrasulfur [2+] cation. Implications for the understanding of the stability of M(4)2+ and M2+ (M = S, Se, and Te) crystalline salts.

S4(AsF6)2.AsF3 was prepared by the reaction of sulfur with arsenic pentafluroide in liquid AsF3 (quantitatively) and in anhydrous HF in the presence of trace amounts of bromine. A single-crystal X-ray structure of the compound has been determined: monoclinic, space group P2(1)/c, Z = 4, a = 7.886(1) A, b = 9.261(2) A, c = 19.191(3) A, beta = 92.82(1) degrees, V = 1399.9(4) A3, T = 293 K, R1 = 0.052 for 1563 reflections (I > 2 sigma (I) 1580 total and 235 parameters). We report a term-by-term calculation of the lattice potential energy of this salt and also use our generalized equation, which estimates lattice energies to assist in probing the homopolyatomic cation thermochemistry in the solid and the gaseous states. We find S4(AsF6)2.AsF3 to be more stable (delta fH degree [S4(AsF6)2.AsF3,c] approximately -4050 +/- 105 kJ/mol) than either the unsolvated S4(AsF6)2 (delta fH degree [S4(AsF6)2,c] approximately -3104 +/- 117 kJ/mol) by 144 kJ/mol or two moles of S2AsF6 (c) and AsF3 (1) by 362 kJ/mol. The greater stability of the S(4)2+ salt arises because of the greater lattice potential energy of the 1:2 solvated salt (1734 kJ/mol) relative to twice that of the 1:1 salt (2 x 541 = 1082 kJ/mol). The relative lattice stabilization enthalpies of M(4)2+ ions relative to two M2+ ions (i.e., in M4(AsF6)2 (c) with respect to two M2AsF6 (c) (M = S, Se, and Te)) are found to be 218, 289, and 365 kJ/mol, respectively. Evaluation of the thermodynamic data implies that appropriate presently available anions are unlikely to stabilize M2+ in the solid phase. A revised value for delta fH degree [Se4(AsF6)2,c] = -3182 +/- 106 kJ/mol is proposed based on estimates of the lattice energy of Se4(AsF6)2 (c) and a previously calculated gasphase dimerization energy of 2Se2+ to Se(4)2+.

Journal Article↗
PubMed2005

Molecular dynamics simulation of the ligand binding domain of farnesoid X receptor. Insights into helix-12 stability and coactivator peptide stabilization in response to agonist binding.

The dynamic changes which take place in the ligand binding domain (LBD) of farneosid X receptor (FXR) in response to agonist binding and in the presence of coactivator peptides were studied with nanosecond time-scale molecular dynamics. Four different systems were analyzed, including the holo-LBD complexed with 6ECDCA, the holo-LBD in the presence of two coactivator peptides, and two artificial apo forms, with and without coactivator peptides. Our results revealed a detailed picture of the differential micro- and macromodifications occurring in the LBD in the presence or not of the agonist molecule and the coactivator peptides. In the apo simulation a major conformational change took place in the crucial helix 12, while the holo-LBD was globally stabilized by the ligand. When the coactivator peptides were included in the simulation, a clear agonist-induced stabilization was observed for the canonical peptide. Interestingly, the second peptide was released from the holo-LBD while it was kept bound in the apo simulation. The present results provide a molecular basis for the understanding the role played by the bile acid agonist in receptor stabilization and enhanced cofactor recruitments.

Binding Sites↗
PubMed2000

Stabilization of proteins encapsulated in cylindrical poly(lactide-co-glycolide) implants: mechanism of stabilization by basic additives.

PURPOSE: A previous study from our group has shown that in the acidic microclimate of poly(lactide-co-glycolide) (PLGA) implants, encapsulated BSA forms insoluble noncovalent aggregates and is hydrolyzed during in vitro release. Incorporation of Mg(OH)2 strongly inhibits these mechanisms of instability and facilitates continuous protein release. The purpose of this study was to determine the protein stabilization mechanism in the presence of basic additives. METHODS: BSA, as a model protein, was encapsulated in PLGA millicylinders by a solvent extrusion method. The release of BSA from the PLGA millicylinders with and without basic additives (Mg(OH)2, Ca(OH)2, ZnCO3 and Ca3(PO4)2) in a physiological buffer was carried out at 37 degrees C and quantified by a modified Bradford assay. The insoluble aggregates extracted from the polymer with acetone were reconstituted in a denaturing (6 M urea) or denaturing/reducing solvent (6 M urea/10 mM DTT) to determine the type of aggregation. RESULTS: Aggregation of encapsulated BSA was inhibited with increasing amount of base co-encapsulated in the polymer, irrespective of the type of base used. The pH drop in the release medium and extent of acid-catalyzed PLGA degradation were both inhibited in the presence of base. The resultant effect was also reflected in an increase in water uptake and porosity of the devices. The inhibition and mechanism of BSA aggregation was correlated with the basicity of the additive. For Ca(OH)2, at 3% loading, covalent BSA aggregation due to thioldisulfide interchange was observed (indicative of ionization of albumin's free thiol at high pH), whereas at 3% ZnCO3 or Ca3(PO4)2, a higher percentage of non-covalent aggregates was observed compared to Mg(OH)2. Decreasing the loading of BSA at constant Mg(OH)2 content caused an increase in BSA aggregation. CONCLUSIONS: The mechanism by which Mg(OH)2 stabilizes encapsulated BSA in PLGA implants is through neutralizing the acidic microclimate pH in the polymer. The successful neutralization afforded by the basic additives requires a percolating network of pores connecting both base and protein. The microclimate pH inside PLGA implants can be controlled by selecting the type of basic salt, which suggests a potential approach to optimize the stability of encapsulated pharmaceuticals in PLGA including therapeutic proteins.

Alkalies↗
PubMed2000

Effects of denaturing and stabilizing agents on the inhibitory activity and conformational stability of Schizolobium parahyba chymotrypsin inhibitor.

The conformational stability of the Schizolobium parahyba chymotrypsin inhibitor (SPCI) was investigated based on conformational changes and inhibitory activity in the presence of chaotropic and stabilizing agents. At 90 degrees C, the half-lifetime of SPCI was 154 min, while in the presence of 1 M KCl and 20% PEG 20,000, it was drastically reduced to 6 and 3 min, respectively. In contrast, at 90 degrees C, the SPCI structure remained unaltered with the addition of 1 mM DTT and 56% glycerol. The reduction of the two disulfide bonds caused conformational changes in the SPCI without altering the inhibitory activity, suggesting that disulfide bonds are irrelevant to the maintenance of SPCI conformation. Unfolded structures were formed in the presence of 6 M GdnHCl, while in the presence of 8 M urea, destabilization was due to peptide bond rupture. These results suggest that the thermal inactivation of SPCI involves conformational changes and that hydrophobic and electrostatic interactions play a significant role, while the disulfide bonds are of secondary importance in maintaining the high thermal stability of SPCI.

Chymotrypsin↗
PubMed2001

[The application of external knee stabilizers - Influence on mechanical stabilization and physical performance].

The aim of the study was, to assess the influence of a knee brace on the development of anterior instability after anterior cruciate ligament rupture and to test aptitude for physical strain. 46 subjects with arthroscopically proven anterior cruciate ligament rupture were divided equally in a randomised order into two groups. Both groups carried out a standardized physical therapy program, while one group (0) received additional stabilization by means of a functional knee brace (SofTec, Bauerfeind). In addition, important features of the brace (stabilization capacity, safety perception and physical performance) were tested and compared to the non-braced contralateral leg among 23 healthy physical education students by means of a standardized scaled questionnaire (observational study). 0 showed lower (p < 0.05) development of the anterior instability by 46 % and lower (p < 0.05) reduction in circumference of the femur muscles by 25 %. Increasing the time interval between accident and beginning of the brace treatment, increased the difference of the therapeutical effect of the brace. In the observational study, the brace received a better evaluation regarding all test parameters. The reduction of developing anterior instability by means of a brace should facilitate - apart from an individual operation-time-arrangement - especially a conservative approach within the framework of anterior instability and physical activity. Aside from the improvement of the mechanical stabilization, indications for suitability in strain situations could be detected for the tested brace.

Adult↗
PubMed1993

Stability of transpedicle screwing for the osteoporotic spine. An in vitro study of the mechanical stability.

The influence of bone mineral density on the stability of transpedicle screwing was studied in the human cadaveric lumbar vertebrae. The pull-out force correlated with bone mineral density. The tilting moment (load needed to tilt the screw 4 degrees cranially at the screw-plate junction) and the cut-up force (load needed to tip the end plate up by the screw) correlated with bone mineral density. A correlation was also found between the maximum insertion torque of the screw and bone mineral density. The maximum insertion torque correlated with the pull-out force, the tilting moment, and the cut-up force. In the cyclic tilting test (200 cycles), the mean value of the tilting moment at the 200th cycle was 67.4 +/- 6.1%, compared with the first cycle. The results suggest that preoperative measurement of BMD is necessary for transpedicle screwing in osteoporotic cases, and that the cyclic tilting motion decrease its mechanical stability. The authors have also concluded that the maximum insertion torque could predict the mechanical stability.

Aged↗
PubMed1999

Computational studies on mutant protein stability: The correlation between surface thermal expansion and protein stability.

Thermal stability of mutant proteins has been investigated using temperature dependent molecular dynamics (MD) simulations in vacuo. The numerical modeling was aimed at mimicking protein expansion upon heating. After the conditions for an expanding protein accessible surface area were established for T4 lysozyme and barnase wild-type proteins, MD simulations were carried out under the same conditions using the crystal structures of several mutant proteins. The computed thermal expansion of the accessible surface area of mutant proteins was found to be strongly correlated with their experimentally measured stabilities. A similar, albeit weaker, correlation was observed for model mutant proteins. This opens the possibility of obtaining stability information directly from protein structure.

Bacterial Proteins↗