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At least 613 records · Page 34Linked to original sources
PubMed1966

Molecular mechanism of red cell "sickling".

Precision scale models of sickle-cell hemoglobin molecules indicate that the genetic substitution of valine for glutamic acid at the 6th position in the two beta chains allows an intramolecular hydrophobic bond to form. This changes the conformation in such a way as to allow molecular stacking. Optical rotatory dispersion studies and the restilts of suLbjection of Hb S solution to temperature change and to propane are consistent with the presence of such a bond. Examination of sickled erythrocytes in a magnetic field and in polarized light indicates that the Hb S molecules are aligned iiz sitil. Filaments interpreted as hollow cables of six Hb S monofilaments have been demonstrated by electron microscopy.

Anemia, Sickle Cell↗
PubMed1968

Protein conformation in solution: cross-linking of lysozyme.

The cross-linking of lysozyme by reaction with phenol-2,4-disulfonyl chloride has been effected. The cross-linked protein retained enzymatic activity, has approximately the same molecular weight as native lysozyme, and has essentially the same conformation as native lysozyme as judged by optical rotatory dispersion analysis. The positions of sulfonylation were assigned by a standard degradation sequence; the presence of sulfonamide bonds was confirmed by infrared spectroscopy. Cross-links may thus be introduced without incurring major structural changes in the protein, and certain intramolecular distances that are allowed in the active enzyme may be deduced.

Amino Acids↗
PubMed1979

Studies on auromomycin.

A new antitumor antibiotic, named auromomycin, was isolated from the culture broth of Streptomyces macromomyceticus, a macromomycin-producing strain. The antibiotic was recovered from the culture filtrate by salting out with ammonium sulfate and further purified by successive application of ion-exchange chromatography on Amberlite IRA-93 (Cl form) and DEAE-Sephadex (OH form), Gel filtration on Sephadex G-50 and hydrophobic chromatography on Octyl-Sepharose CL-4B. The antibiotic is an acidic polypeptide with a molecular weitht of 12,500 and an isoelectric point of pH 5.4 and consists of 16 different amino acids. It has characteristic absorption maxima at 273 nm and 357 nm in the ultraviolet spectrum and two minima at 280 nm and 350 nm in the optical rotatory dispersion spectrum. Auromomycin exhibits antibacterial activity not only against Gram-positive bacteria, but also Gram-negative bacteria. Antitumor activities of auromomycin were revealed against EHRLICH ascites carcinoma, ascites sarcoma 180, L1210 leukemia and LEWIS lung carcinoma. Auromomycin was found to be converted into macromomycin by adsorption chromatography on Amberlite XAD.

Amino Acids↗
PubMed1975

Purification properties and subunit composition of pig heart lipoate acetyltransferase.

Lipoate acetyltransferase [acetyl-CoA: dihydrolipoate S-acetyl-transferase, EC 2.3.1.12], the core enzyme of the pyruvate dehydrogenase complex, has been highly purified by gel chromatography on Sepharose 6B and sucrose density gradient centrifugation in the presence of potassium iodide. The native enzyme has a sedimentation coefficient (S020,W) of 26.7S and a diffusion coefficient (D020,W) of 1.25 x 10(-7) cm2.-sec-1. The weight-average molecular weight was estimated to be 1.8 million from the sedimentation equilibrium data. The content of right-handed alpha helix in the enzyme molecule was estimated to be about 25% by optical rotatory dispersion and about 22% from the circular dichroism spectra. The enzyme was found to contain about 23 moles of protein-bound lipoic acid per mole of enzyme; some other properties are also reported. Lipoate acetyltransferase dissociated to yield a single subunit with a molecular weight of 74,000 as estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and by gel filtration on Bio-Gel in 6 M guanidine-HCl. The molecular weight was also estimated to be 74,000 from sedimentation equilibrium data in 6 M guanidine-HCl] containing 0.1 M 2-mercaptoethanol. Evidence is presented that 1 molecule of lipoate acetyltransferase apparently consists of 24 very similar subunits, each of which contains NH2-terminal alanine. Each subunit contains 1 molecule of covalently bound lipoic acid.

Acetyltransferases↗
PubMed1990

Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagens alpha 1(2) alpha 2 and alpha 1 alpha 2 alpha 3.

The thermal triple helix to coil transitions of two human type V collagens (alpha 1(2) alpha 2 and alpha 1 alpha 2 alpha 3) and bovine type XI collagen differ from those of the interstitial collagens type I, II, and III by the presence of unfolding intermediates. The total transition enthalpy of these collagens is comparable to the transition enthalpy of the interstitial collagens with values of 17.9 kJ/mol tripeptide units for type XI collagen, 22.9 kJ/mol for type V (alpha 1(2) alpha 2), and 18.5 kJ/mol for type V (alpha 1 alpha 2 alpha 3). It is shown by optical rotatory dispersion and differential scanning calorimetry that complex transition curves with stable intermediates exist. Type XI collagen has two main transitions at 38.5 and 41.5 degrees C and a smaller transition at 40.1 degrees C. Type V (alpha 1(2) alpha 2) shows two main transitions at 38.2 and 42.9 degrees C and two smaller transitions at 40.1 and 41.3 degrees C. Compared to these two collagens type V (alpha 1 alpha 2 alpha 3) unfolds at a lower temperature with two main transitions at 36.4 and 38.1 degrees C and two minor transitions at 40.5 and 42.9 degrees C. The intermediates present at different temperatures are characterized by resistance to trypsin digestion, length measurements of the resistant fragments after rotary shadowing, and amino-terminal sequencing. One of the intermediate peptides has been identified as belonging to the alpha 2 type V chain, starting at position 430 and being about 380 residues long. (The residue numbering begins with the first residue of the first amino-terminal tripeptide unit of the main triple helix. The alpha 2(XI) chain was assumed to be the same length as the alpha 1(XI). One intermediate was identified from the alpha 2(XI) chain and with starting position at residue 495, and three from the alpha 3(XI) with starting positions at residues 519, 585, and 618.

Amino Acid Sequence↗
PubMed1986

Amino acid sequence of Escherichia coli glutamine synthetase deduced from the DNA nucleotide sequence.

Glutamine synthetase is encoded by the glnA gene of Escherichia coli and catalyzes the formation of glutamine from ATP, glutamate, and ammonia. A 1922-base pair fragment from a cDNA containing the glnA structural gene for E. coli glutamine synthetase has been sequenced. An open reading frame of 1404 base pairs encodes a protein of 468 amino acid residues with a calculated molecular weight of 51,814. With few exceptions, the amino acid sequence deduced from the DNA sequence agreed very well with the amino acid sequences of several peptides reported previously. The secondary structure predicted for the E. coli enzyme has approximately 36% of the residues in alpha-helices which is in agreement with calculations of approximately 39% based on optical rotatory dispersion data. Comparison of the amino acid sequences of glutamine synthetase from E. coli (468 amino acids) and Anabaena (473 amino acids) (Turner, N. E., Robinson, S. T., and Haselkorn, R. (1983) Nature 306, 337-342) indicates that 260 amino acids are identical and 80 are of the same type (polar or nonpolar) when aligned for maximum homology. Several homologous regions of these two enzymes exist, including the sites of adenylylation and oxidative modification, but the regulation of each enzyme is different.

Amino Acid Sequence↗
PubMedDate not supplied

[Effect of polymer modification of insulin on its enzymatic hydrolysis and conformation properties].

AI, B29 insulin polymeric derivatives in which the polymeric chains (N-polyvinylimidazole, N-polyvinylpyrrolydone and polyacrylic acid) are bonded to the insulin molecule at one point were synthesized. The hydrolysis of the modified insulin by trypsin is dependent to a great extent on the chemical nature of the modifying polymer and is virtually independent of its molecular weight up to 20 kD. The effect of the modifying polymer manifests itself mainly in a change of the Michaelis constant. Investigation of the conformational properties of the insulin derivatives by the method of optical rotatory dispersion revealed that insulin modification by polymers caused a decrease of the amino acid content in the alpha-helical sequence from 41 to 33-30%. The chemical nature of the modifying polymer and its molecular weight have a profound effect on the conformational stability of the residual spatial structure of the modified insulin in alkaline media.

Amino Acids↗
PubMed1987

The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.

Peptidyl-prolyl cis-trans isomerase was extracted from pig kidney cortex and partially purified. Enzyme activity was monitored against the cis-trans isomerization of succinyl-Ala-Ala-Pro-Phe-methylcoumaryl amide by means of a two-step process using chymotrypsin as the trans cleaving activity. The in vitro refolding of denatured type III collagen, which is rate-limited by the cis-trans isomerization of peptide bonds, was studied in the presence of peptidyl-prolyl cis-trans isomerase by optical rotatory dispersion and by resistance to tryptic digestion. A 3-fold increase in the initial rate of folding was observed compared to the uncatalyzed refolding. This rate increase is comparable to the rate increase found for the CT-phase in the refolding of urea-denatured ribonuclease A, but it is smaller than the increase in the rate of isomerization of succinyl-Ala-Ala-Pro-Phe-methylcoumarylamide.

Amino Acid Isomerases↗
PubMed1983

Detection of D-erythro and L-threo sphingosine bases in preparative sphingosylphosphorylcholine and its N-acylated derivatives and some evidence of their different chemical configurations.

Sphingosylphosphorylcholine prepared from native sphingomyelin by the Kaller procedure was found to comprise about 70% of the L-threo (2S, 3S) isomer and 30% of the D-erythro (2S, 3R) isomer. This analytical result was obtained by gas-liquid chromatography (GLC) of trimethylsilyl derivatives of N-acetylsphingosines which were prepared by enzymatic hydrolysis of synthetic N-acetylsphingosylphosphorylcholines with Clostridium perfringens phospholipase C. Some other evidence of the different chemical configuration between the erythro and threo isomers of synthetic N-acylated sphingosylphosphorylcholines was also provided by thin layer chromatography (TLC), optical rotatory dispersion (ORD), and fast atom bombardment (FAB) mass spectrometry.

Acylation↗
PubMedDate not supplied

[The role of the structural organization of apoprotein E in cholesterol binding].

The ability of some proteins to bind cholesterol was accompanied by a decrease of turbidity of aqueous cholesterol suspensions and correlated with a quantity of arginine residues in them. Maximum clearing of aqueous cholesterol suspensions at the addition of proteins containing equimolar arginine concentrations was observed in the presence of apoproteins E and A-I. Optical rotatory dispersion spectra of apoprotein E, polyarginine and histone H3 have shown the influence of sterol on the secondary structure of apoprotein E only.

Apolipoproteins↗
PubMed1982

1H-NMR studies of the structure and stability of the bovine pancreatic secretory trypsin inhibitor.

The tertiary structure of the isoinhibitor A (Kazal) isolated from bovine pancreatic tissue has been characterized by 1H-NMR studies in 2H2O solution. A number of slowly exchanging backbone amides are observed. The dynamics of the aromatic side chains and their interaction with methyl groups from aliphatic residues are essentially identical in the bovine and in the homologous inhibitor from porcine pancreas. Both inhibitors contain two tyrosines in positions 20 and 31 as the only aromatic residues. The previous assignment of the aromatic resonances in the porcine inhibitor is valid for the bovine homolog, as deduced from selective nuclear Overhauser enhancement (NOE) experiments. The tyrosine which inhibits an NMR spectral pattern characteristic of rapid ring motion does not show appreciable NOE to backbone or sidechain protons, in agreement with the solvent exposure predicted for Tyr-20 in the porcine inhibitor. In contrast, the immobilized Tyr-31 exhibits a NOE pattern that indicates close interaction with a number of backbone amide protons and aliphatic side chain groups, confirming that the aromatic ring is buried. At 90 degrees C, pH 5, the protein is still substantially folded, as manifested by both backbone and side chain resonances. The results are compared with previous optical rotatory dispersion findings. A number of side chain resonances were assigned to specific amino acid residues in the sequence.

Amino Acid Sequence↗
PubMed1993

Hysteresis in the triple helix-coil transition of type III collagen.

A hysteresis is observed in the triple helix-coil transition of type III collagen. This hysteresis appears in the thermal transition, where it is not solvent-dependent, and also in the transition induced by guanidinium hydrochloride. The transitions are observed both by optical rotatory dispersion and by trypsin digestion. Experiments with various fragments of type III collagen, which, like the intact protein, contain a set of disulfide bonds at the carboxyl-terminal end, which functions as an effective nucleus for refolding, indicate that the hysteresis depends on the amino acid sequence, rather than being a general property of the triple helix. The carboxyl-terminal one-quarter fragment of type III collagen does not show a hysteresis, whereas a mutant type III collagen missing residues 595-1008 shows a hysteresis of the same magnitude as normal type III collagen. Several fragments were produced that are missing parts of the amino-terminal end, and these fragments show no hysteresis. The amino-terminal part of the triple helix of type III collagen consists of a stable region containing six Gly-Pro-Hyp tripeptide units within the first 16 tripeptide units. This region forms an amino-terminal clamp for the triple helix and, together with the set of disulfide bonds at the carboxyl-terminal end, allows for highly cooperative unfolding of the triple helix. The presence of this amino-terminal region is a prerequisite for the observed hysteresis.

Amino Acid Sequence↗
PubMed1996

[Partially unfolded state of lysozyme with a developed secondary structure in dimethylsulfoxide].

The conformation of a chicken egg lysozyme molecule (dimensions, stoichiometry of its associates, and the degree of helicity) in DMSO was studied by small-angle neutron scattering, dynamic light scattering, and optical rotatory dispersion in the visible region of the spectrum. At high DMSO concentrations (70%), the protein was shown to exist as a dimer. The monomer molecules in the dimer adopt a partially unfolded conformation, with dimensions substantially greater than those in the native state and a high content of secondary structure (the degree of helicity is close to that of native lysozyme). This approach provides a unique possibility to assess the compactness of molecules in associates, which may be very useful in studying protein self-organization.

Animals↗
PubMed1970

Congo red dichroism with dispersed amyloid fibrils, an extrinsic cotton effect.

The spectral absorption, optical rotatory dispresion, and circular dichroism associated with interaction of Congo red dye with partly purified suspensions of amyloid fibril fragments were examined. A set of phenomena consistent with a Cotton effect was found. A nearly identical set of phenomena was obtained with poly-L-lysine in its alpha-helical form. The dichroism seen when Congo red binds to amyloid substance in tissue sections can also be interpreted as a Cotton effect. This suggests that some special conformation, presumably in protein, is present in a major constituent of amyloid. This conformation is not present in gamma globulin, Bence-Jones protein, albumin, fibrinogen, or other proteins tested so far. These and other optical properties of amyloid substance can be used to compare amyloid deposits in different human cases and in different species. Extension of the use of polarization microscopy with other dyes that bind to other substances in tissue sections should permit more exquisite probing of the conformation of important macromolecules in situ in cells and tissues than has hitherto been possible.

Amyloid↗