Opredelenie i sravnitel'nyǐ analiz konformatsiǐ ostova belkovykh molekul bych'ego pankreaticheskogo ingibitora tripsina i ingibitorov tripsina E i K na osnove dannykh dvumernoǐ 1H-IaMR-spektroskopii.

Translated title of the contribution: Determination and comparative analysis of the conformation of bovine pancreatic trypsin inhibitor and trypsin inhibitors E and K from the data of two-dimensional 1H-NMR spectroscopy

S. A. Sherman, A. M. Andrianov

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

On the basis of joint consideration of distance dependences between amide proton NH and protons C alpha H, NH, C beta H of the preceding in amino acid sequence residue from the torsion angles phi psi, chi 1, the correlation diagram of these proton-proton distances with the regions of sterically allowed conformational space (phi, psi) is presented and the method for the determination of the L-amino acid residues backbone conformations is proposed. The diagram was used for the determination of backbone conformations of bovine pancreatic trypsin inhibitor and trypsin inhibitors E and K from Dendroaspis polylepis using the data from two-dimensional 1H-NMR spectroscopy. The analysis of backbone conformations was carried out. The individual elements of these protein molecules secondary structure were characterized and their high conformational homology was shown. The inference about qualitative coincidence of three protein molecules conformation in solution, preservation of secondary structure basic elements and their similarity with bovine pancreatic trypsin inhibitor crystalline structure was made.

Original languageRussian
Pages (from-to)1301-1309
Number of pages9
JournalMolekuliarnaia biologiia
Volume19
Issue number5
StatePublished - Sep 1 1985

Fingerprint

Aprotinin
Protons
Magnetic Resonance Spectroscopy
Secondary Protein Structure
Elapidae
Protein Conformation
Amides
Amino Acid Sequence
Joints
Amino Acids
Proton Magnetic Resonance Spectroscopy
isoinhibitor K

ASJC Scopus subject areas

  • Medicine(all)

Cite this

@article{50d3595a7e3d44918cf0944877fdee97,
title = "Opredelenie i sravnitel'nyǐ analiz konformatsiǐ ostova belkovykh molekul bych'ego pankreaticheskogo ingibitora tripsina i ingibitorov tripsina E i K na osnove dannykh dvumernoǐ 1H-IaMR-spektroskopii.",
abstract = "On the basis of joint consideration of distance dependences between amide proton NH and protons C alpha H, NH, C beta H of the preceding in amino acid sequence residue from the torsion angles phi psi, chi 1, the correlation diagram of these proton-proton distances with the regions of sterically allowed conformational space (phi, psi) is presented and the method for the determination of the L-amino acid residues backbone conformations is proposed. The diagram was used for the determination of backbone conformations of bovine pancreatic trypsin inhibitor and trypsin inhibitors E and K from Dendroaspis polylepis using the data from two-dimensional 1H-NMR spectroscopy. The analysis of backbone conformations was carried out. The individual elements of these protein molecules secondary structure were characterized and their high conformational homology was shown. The inference about qualitative coincidence of three protein molecules conformation in solution, preservation of secondary structure basic elements and their similarity with bovine pancreatic trypsin inhibitor crystalline structure was made.",
author = "Sherman, {S. A.} and Andrianov, {A. M.}",
year = "1985",
month = "9",
day = "1",
language = "Russian",
volume = "19",
pages = "1301--1309",
journal = "Molekulyarnaya Biologiya",
issn = "0026-8984",
publisher = "Russian Academy of Sciences",
number = "5",

}

TY - JOUR

T1 - Opredelenie i sravnitel'nyǐ analiz konformatsiǐ ostova belkovykh molekul bych'ego pankreaticheskogo ingibitora tripsina i ingibitorov tripsina E i K na osnove dannykh dvumernoǐ 1H-IaMR-spektroskopii.

AU - Sherman, S. A.

AU - Andrianov, A. M.

PY - 1985/9/1

Y1 - 1985/9/1

N2 - On the basis of joint consideration of distance dependences between amide proton NH and protons C alpha H, NH, C beta H of the preceding in amino acid sequence residue from the torsion angles phi psi, chi 1, the correlation diagram of these proton-proton distances with the regions of sterically allowed conformational space (phi, psi) is presented and the method for the determination of the L-amino acid residues backbone conformations is proposed. The diagram was used for the determination of backbone conformations of bovine pancreatic trypsin inhibitor and trypsin inhibitors E and K from Dendroaspis polylepis using the data from two-dimensional 1H-NMR spectroscopy. The analysis of backbone conformations was carried out. The individual elements of these protein molecules secondary structure were characterized and their high conformational homology was shown. The inference about qualitative coincidence of three protein molecules conformation in solution, preservation of secondary structure basic elements and their similarity with bovine pancreatic trypsin inhibitor crystalline structure was made.

AB - On the basis of joint consideration of distance dependences between amide proton NH and protons C alpha H, NH, C beta H of the preceding in amino acid sequence residue from the torsion angles phi psi, chi 1, the correlation diagram of these proton-proton distances with the regions of sterically allowed conformational space (phi, psi) is presented and the method for the determination of the L-amino acid residues backbone conformations is proposed. The diagram was used for the determination of backbone conformations of bovine pancreatic trypsin inhibitor and trypsin inhibitors E and K from Dendroaspis polylepis using the data from two-dimensional 1H-NMR spectroscopy. The analysis of backbone conformations was carried out. The individual elements of these protein molecules secondary structure were characterized and their high conformational homology was shown. The inference about qualitative coincidence of three protein molecules conformation in solution, preservation of secondary structure basic elements and their similarity with bovine pancreatic trypsin inhibitor crystalline structure was made.

UR - http://www.scopus.com/inward/record.url?scp=0022126073&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022126073&partnerID=8YFLogxK

M3 - Article

C2 - 4079926

AN - SCOPUS:0022126073

VL - 19

SP - 1301

EP - 1309

JO - Molekulyarnaya Biologiya

JF - Molekulyarnaya Biologiya

SN - 0026-8984

IS - 5

ER -