(v. t.) To lap or lay in plaits or folds; to lay one part over another part of; to double; as, to fold cloth; to fold a letter.
(v. t.) To double or lay together, as the arms or the hands; as, he folds his arms in despair.
(v. t.) To inclose within folds or plaitings; to envelop; to infold; to clasp; to embrace.
(v. t.) To cover or wrap up; to conceal.
(v. i.) To become folded, plaited, or doubled; to close over another of the same kind; to double together; as, the leaves of the door fold.
(v.) A doubling,esp. of any flexible substance; a part laid over on another part; a plait; a plication.
(v.) Times or repetitions; -- used with numerals, chiefly in composition, to denote multiplication or increase in a geometrical ratio, the doubling, tripling, etc., of anything; as, fourfold, four times, increased in a quadruple ratio, multiplied by four.
(v.) That which is folded together, or which infolds or envelops; embrace.
(n.) An inclosure for sheep; a sheep pen.
(n.) A flock of sheep; figuratively, the Church or a church; as, Christ's fold.
(n.) A boundary; a limit.
(v. t.) To confine in a fold, as sheep.
(v. i.) To confine sheep in a fold.
Example Sentences:
(1) Patient plasma samples demonstrated evidence of marked complement activation, with 3-fold elevations of C3a desArg concentrations by the 8th day of therapy.
(2) 5-Azacytidine (I) stability was increased approximately 10-fold over its stability in water or lactated Ringer injection by the addition of excess sodium bisulfite and the maintenance of pH approximately 2.5.
(3) Radioligand binding studies revealed the presence of a single class of high-affinity (Kd = 2-6 X 10(-10) M) binding sites for ET-1 in both cells, although the maximal binding capacity of cardiac receptor was about 6- to 12-fold greater than that of vascular receptor.
(4) The enzyme was solubilized by Triton X-100 and purified approximately 480-fold by gel filtration and affinity chromatography on alanine methyl ketone-AH-Sepharose 4B.
(5) The DNA untwisting enzyme has been purified approximately 300-fold from rat liver nuclei.
(6) IP3 increased 1.7-fold and IP2 1.6-fold after 20 and 40 s, respectively.
(7) Short incubations with heparin (5 min) caused a release of the enzyme into the media, while longer incubations caused a 2-8-fold increase in net lipoprotein lipase secretion which was maximal after 2-16 h depending on cell type, and persisted for 24 h. The effect of heparin was dose-dependent and specific (it was not duplicated by other glycosaminoglycans).
(8) The following conclusions emerge: (i) when the 3' or the 3' penultimate base of the oligonucleotide mismatched an allele, no amplification product could be detected; (ii) when the mismatches were 3 and 4 bases from the 3' end of the primer, differential amplification was still observed, but only at certain concentrations of magnesium chloride; (iii) the mismatched allele can be detected in the presence of a 40-fold excess of the matched allele; (iv) primers as short as 13 nucleotides were effective; and (v) the specificity of the amplification could be overwhelmed by greatly increasing the concentration of target DNA.
(9) Epicanthal folds were present in 46%, mongoloid slanting of the lids in 72% of cases.
(10) The estimated DNA compaction ratio (approximately 3-fold) is consistent with a significant degree of nucleosome unfolding in the hyperstimulated BR genes.
(11) Two hours after refeeding rats fasted for 48 h, ODC activity increased 40-fold in mucosa from the intact jejunum and 4-fold in the mucosa of the bypassed segments.
(12) Transfection of the treated DNA into SOS-induced spheroplasts results in an increase in mutagenesis as great as 50-fold.
(13) ACh released from the vesicular fraction was about 100-fold more than could be accounted for by miniature end-plate potentials; possible causes of this overestimate are discussed.
(14) In strains completely deleted for galR, the gene which encodes the Gal repressor, the operon is derepressed by only 10-fold without an inducer.
(15) The amount of water, creatinine, electrolytes, proteins, and enzymes were higher during the day (up to three fold, p always less than 0.05), while equal amounts of amino acids were excreted in the day and the night period.
(16) TNBS reacts to an extremely small extend with hemoglobin over the concentration range 0.4 to 4 mM whereas FDNB reacts with hemoglobin to a very large extent (50 fold more than TNBS).
(17) Rates of PC in vitro metabolism by liver and kidney cytosolic cysteine conjugate beta-lyases (beta-lyases) were similar, but metabolism by renal mitochondrial beta-lyase occurred at a 3-fold higher rate than the rate obtained with hepatic mitochondrial beta-lyase.
(18) Dietary factors affect intestinal P450s markedly--iron restriction rapidly decreased intestinal P450 to beneath detectable values; selenium deficiency acted similarly but was less effective; Brussels sprouts increased intestinal AHH activity 9.8-fold, ECOD activity 3.2-fold, and P450 1.9-fold; fried meat and dietary fat significantly increased intestinal EROD activity; a vitamin A-deficient diet increased, and a vitamin A-rich diet decreased intestinal P450 activities; and excess cholesterol in the diet increased intestinal P450 activity.
(19) On the other hand, if we correct for the population of HMM with degraded light chain 2, the difference in the binding constants in the presence and absence of Ca2+ may be as great as 5-fold.
(20) The gene, which is located at chromosome XIII, is transcribed as a mRNA of about 2.7 kilobases, and the amount of message has been found to increase 3- to 4-fold during the culture.
Refold
Definition:
(v. t.) To fold again.
Example Sentences:
(1) Refolding was observed by injection of denatured protein into columns having isocratic concentrations in the transition and native base-line zones.
(2) Both enzymes are capable of catalyzing the refolding of thermally denatured type III collagen.
(3) Air-regenerated monomers of bovine seminal ribonuclease have been found capable of reassociating into native dimers, whereas monomers refolded in the presence of a glutathione redox mixture do not reassociate into dimers [Smith, K. G., D'Alessio, G. and Schaffer, S. W. (1978) Biochemistry 17, 2633-2638].
(4) When samples at pH 3.5 were dialyzed against 0.1 M ammonium acetate (pH 6.9) to refold interferon gamma, the samples that contained NaCl in acid formed aggregates upon dialysis while those without NaCl formed a dimer apparently identical with the starting protein (i.e., before acid treatment).
(5) When refolding is performed in the presence of methotrexate, an analogue of dihydrofolate, and NADPH, NADPH binds, as determined from changes in NADPH fluorescence, to the third observed intermediate rather than the last (fourth) species formed.
(6) In contrast, import of the surface-bound unfolded precursor requires ATP, but no potential; it is accompanied by a refolding inside the mitochondria.
(7) In the present study, the reversibility of the unfolding-refolding process induced by guanidine hydrochloride was investigated for the intact protein and the isolated domains.
(8) Convenient and rapid assays for detecting native protein are critical for developing a refolding procedure.
(9) In vitro refolding of the urea-unfolded, monomeric, mitochondrial enzyme rhodanese (thiosulfate sulfur-transferase; EC 2.8.1.1) is facilitated by the chaperonin proteins cpn60 and cpn10 from Escherichia coli at 37 degrees C, but the refolding is strongly inhibited at 10 degrees C. In contrast, the unassisted refolding of rhodanese is efficient at 10 degrees C, but the refolding efficiency decreases as the temperature is raised.
(10) Furthermore, the necessity to reactivate proteins at low protein concentrations due to its tendency to aggregate at high concentrations was overcome by a step-by-step addition of denatured and reduced protein into the refolding solution.
(11) (1990) Biochemistry (preceding paper in this issue)] were used to propose kinetic models for the unfolding and refolding of ribonuclease T1.
(12) The fractional renaturation of rhodanese due to the fast phase, monitored in various concentrations of GdmCl, describes a transition centered at 3.5 M GdmCl which is very similar to the higher of the two transitions observed in the reversible refolding.
(13) At dilute protein concentrations the refolding can be studied independent of the association phenomena.
(14) The effect of protein concentration and denaturant concentration on the kinetics of refolding were studied.
(15) Thus, the absence of a covalent linkage between the two proteolytic fragments of the enzyme molecule apparently does not affect the refolding.
(16) Downstream processing of the fusion proteins involved isolation of inclusion bodies, cleavage at the Asn-Gly bond, refolding of the reduced IGF-I peptide and purification to homogeneity.
(17) It appeared that the virus protein coat was sufficiently plastic so that the initial conformational change resulting from the alteration of an arginine residue (to possibly an ornithine residue) was at least partially reversible and that the virus tail proteins then refolded to produce a stable and active virus particle.
(18) This approach was found to be effective in minimizing the refolding difficulties and allowed accessibility to the synthesis of analogues in this class of compounds.
(19) At high temperatures above 60 degrees C, where the native enzymes are stable but their spontaneous refoldings upon dilution of guanidine HCl fail, the chaperonin induces productive refolding in an ATP-dependent manner.
(20) Over a period of several hours, refolded and inactive prorenin not bound to the column slowly regains 5% to 10% renin activity, even when maintained under conditions that are optimal for zymogen inactivation.