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1.

Study of the infrared spectra of oligosaccharides in the region 1,000-40 cm-1.

Tul'chinsky, V M; Zurabyan, S E; Asankozhoev, K A; Kogan, G A; Khorlin, A Y.

Carbohydr Res ; 51(1): 1-8, 1976 Oct.

Article in English | MEDLINE | ID: mdl-1000524

ABSTRACT

The i.r. spectra of disaccharides differing in monosaccharide composition and in the position and configuration of the glycosidic linkage, and also those of raffinose and model saccharides, were studied in the region 1,000-40 cm-1. Two ranges may be of interest for structural analysis. The first, called "the anomeric region=, is suitable for the determination of the configuration of the glycosidic linkage. The spectra of the oligosaccharides in the second region, called "the region of crystallinity", depend upon the packing of the molecules in the solid. The reasons for the present impossibility of using the far-infrared region of the i.r. spectra of lower oligosaccharides for the determination of the position of the glycosidic linkage are considered.

Subject(s)

Oligosaccharides , Binding Sites , Crystallization , Molecular Conformation , Spectrophotometry, Infrared

2.

Steric analysis of glycerophospholipids by circular dichroism. Stereospecifity of phospholipase D catalyzed transesterification.

Batrakov, S G; Panosyan, A G; Kogan, G A; Bergelson, L D.

Biochem Biophys Res Commun ; 66(2): 755-62, 1975 Sep 16.

Article in English | MEDLINE | ID: mdl-1237303

Subject(s)

Glycerides , Phospholipases , Phospholipids , Circular Dichroism , Egg Yolk , Female , Molecular Conformation , Phosphatidylcholines , Phospholipases/metabolism , Plants/enzymology , Structure-Activity Relationship

3.

A study of the conformational states of aspartate aminotransferase by perturbation spectrophotometry. I. The change in the accessibility of the coenzyme during the enzymatic reaction.

Bocharov, A L; Kogan, G A.

Mol Biol ; 8(3): 355-61, 1974 Nov.

Article in English | MEDLINE | ID: mdl-4474587

Subject(s)

Aspartate Aminotransferases , Pyridoxal Phosphate , Animals , Aspartate Aminotransferases/metabolism , Aspartic Acid/analogs & derivatives , Binding Sites , Cycloserine , Ethylene Glycols , Myocardium/enzymology , Protein Binding , Protein Conformation , Spectrophotometry , Spectrophotometry, Ultraviolet , Swine

4.

[Conformational states of aspartate-aminotransferase as studied by solvent perturbation difference spectroscopy. II. Perturbation of the UV-absorption spectra of the protein by the coenzyme and ethylene glycol]. / Izuchenie konformatsionnykh sostoianii aspartat-aminotransferazy metodom perturbatsionnoi spektrofotometrii. II. Perturbatsiia UF-spektrov belka v oblasti pogloshcheniia aromaticheskikh aminokislot pod vliianiem etilenglikolia i kofermenta

Kogan, G A; Bocharov, A L; Karpeiskii, M Ia.

Mol Biol ; 8(5): 762-7, 1974.

Article in Russian | MEDLINE | ID: mdl-4469584

Subject(s)

Aspartate Aminotransferases , Ethylene Glycols , Pyridoxal Phosphate , Apoenzymes , Aspartate Aminotransferases/analysis , Binding Sites , Protein Binding , Protein Conformation , Spectrophotometry, Ultraviolet , Tryptophan/analysis , Tyrosine/analysis

5.

Depsipeptide modification as a method of determining the contribution of intramolecular hydrogen bonds to the conformational stability of peptides (gramicidin S).

Zhuze, A L; Kogan, G A; Krit, N A; Andronova, T M; Filatova, M P; Senyavina, L B; Meshcheryakova, E A; Ryabova, I D; Ravdel', G A; Shchukina, L A.

Mol Biol ; 8(1): 69-74, 1974 Jul.

Article in English | MEDLINE | ID: mdl-4139643

Subject(s)

Gramicidin , Peptides, Cyclic , Circular Dichroism , Molecular Conformation , Spectrophotometry, Infrared , Spectrophotometry, Ultraviolet

6.

A circular dichroism study of lactosomatotropin, bovine lactogenic hormone, and the products of their chemical modification at a tyrosine residue.

Kogan, G A; Nagornaya, L V; Ryshka, F Y; Khokhlov, A S.

Mol Biol ; 7(5): 570-4, 1974 Mar.

Article in English | MEDLINE | ID: mdl-4825843

Subject(s)

Pituitary Hormones, Anterior , Animals , Cattle , Circular Dichroism , Molecular Conformation , Prolactin

7.

Chromophore labels in proteins. II. pH-dependence of circular dichroic spectra and differential perturbation spectra of alpha-chymotrypsin.

Kogan, G A; Chekhlyaeva, N M; Slobodyanskaya, E M; Kozlov, L V; Antonov, V K.

Mol Biol ; 7(4): 485-9, 1974 Jan.

Article in English | MEDLINE | ID: mdl-4824809

Subject(s)

Chymotrypsin , Chromatography, Gel , Chromatography, Ion Exchange , Circular Dichroism , Ethylenes , Glycols , Hydrogen-Ion Concentration , Protein Conformation , Spectrophotometry, Ultraviolet , Urea

8.

Chromophore labels in proteins. 3. Differential perturbation spectra and circular dichroic spectra of alpha-chymotrypsin modified by nitration.

Slobodyanskaya, E M; Kogan, G A; Kozlov, L V; Volkova, L I; Antonov, V K.

Mol Biol ; 7(4): 490-5, 1974 Jan.

Article in English | MEDLINE | ID: mdl-4824810

Subject(s)

Chymotrypsin , Nitro Compounds , Amides , Buffers , Circular Dichroism , Citrates , Ethylenes , Glycine , Glycols , Hydrogen-Ion Concentration , Optical Rotation , Protein Conformation , Spectrophotometry , Spectrophotometry, Ultraviolet , Tyrosine

9.

The far-infrared spectra of alkali metal ion complexes with valinomycin, beauvericin, nonactin and perhydroantamanide in solution.

Ivanov, V T.; Kogan, G A.; Tulchinsky, V M.; Miroshnikov, A V.; Mikhalyova, I I.; Evstratov, A V.; Zenkin, A A.; Kostetsky, P V.; Ovchinnikov, Yu A.; Lokshin, B V..

FEBS Lett ; 30(2): 199-204, 1973 Mar 01.

Article in English | MEDLINE | ID: mdl-11947093

10.

[Spectrophotometric determination of glutamate decarboxylase activity]. / Spektrofotometricheskoe opredelenie aktivnosti glutamatdekarboksilazy.

Torchinskii, Iu M; Mekhanik, M L; Kogan, G A.

Dokl Akad Nauk SSSR ; 205(3): 731-3, 1972 Jul 21.

Article in Russian | MEDLINE | ID: mdl-4563948

Subject(s)

Carboxy-Lyases , Escherichia coli/enzymology , Glutamates , Methods , Spectrophotometry, Ultraviolet

11.

[Effect of dimethyl sulfoxide on the secondary structure of globular proteins]. / Vliianie dimetilsul'foksida na vtorichnuiu strukturu nekotorykh golbuliarnykh belkov.

Khurgin, Iu I; Azizov, Iu M; Abaturov, L V; Kogan, G A; Rosliakov, V Ia.

Biofizika ; 17(3): 390-5, 1972.

Article in Russian | MEDLINE | ID: mdl-5042284

Subject(s)

Dimethyl Sulfoxide , Enzymes , Proteins , Chymotrypsin , Chymotrypsinogen , Globins , Hemoglobins , Infrared Rays , Insulin , Muramidase , Optical Rotatory Dispersion , Peroxidases , Protamines , Spectrum Analysis , Trypsin

12.

Chromophoric labels in proteins. I. Optical and luminescent properties of nitrochymotrypsin and nitrochymotrypsinogen.

Surovaya, A N; Slobodyanskaya, E M; Kozlov, L V; Kogan, G A; Antonov, V K.

Mol Biol ; 6(1): 85-90, 1972.

Article in English | MEDLINE | ID: mdl-5086744

Subject(s)

Chymotrypsin , Chymotrypsinogen , Protein Conformation , Acetates , Catalysis , Chymotrypsin/antagonists & inhibitors , Circular Dichroism , Hydrogen-Ion Concentration , Luminescent Measurements , Mathematics , Nitro Compounds , Optical Rotatory Dispersion , Protein Binding , Spectrometry, Fluorescence , Spectrophotometry , Tyrosine , Ultraviolet Rays

13.

Spectra of methylamides of N-acetyl-L-alanine and N-acetyl-L-valine in the middle and far infrared regions.

Kogan, G A; Tul'chinskii, V M; Kostetskii, P V; Miroshnikov, A I.

Mol Biol ; 5(6): 743-9, 1971.

Article in English | MEDLINE | ID: mdl-5155110

Subject(s)

Alanine , Amides , Spectrophotometry, Infrared , Valine , Acetates , Chemical Phenomena , Chemistry , Deuterium , Methylation , Optical Rotation , Protein Conformation

14.

Application of optical rotatory dispersion to the study of pituitary protein hormones.

Ryshka, F Y; Kogan, G A; Struchkova, M I.

Mol Biol ; 5(3): 392-5, 1971.

Article in English | MEDLINE | ID: mdl-5154833

Subject(s)

Optical Rotatory Dispersion , Pituitary Hormones , Protein Conformation , Animals , Cattle , Chromatography, Gel , Chromatography, Ion Exchange , Electrophoresis, Starch Gel , Follicle Stimulating Hormone , Growth Hormone , Hydrogen-Ion Concentration , Luteinizing Hormone , Methods , Molecular Weight , Phenylalanine , Threonine , Ultracentrifugation , Ultraviolet Rays , Urea

15.

[Nitration of tyrosine residues in pepsin by tetranitromethane]. / Nitrovanie tirozinovykh ostatkov v pepsine tetranitrometanom.

Kozlov, L V; Kogan, G A; Zavada, L L.

Biokhimiia ; 34(6): 1257-65, 1969.

Article in Russian | MEDLINE | ID: mdl-4907344

Subject(s)

Alkanes , Pepsin A , Tyrosine , Chemical Phenomena , Chemistry , Dipeptides , Hemoglobins , Kinetics , Models, Biological , Models, Structural , Optical Rotatory Dispersion , Spectrum Analysis , Thermodynamics , Time Factors , Ultraviolet Rays

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