About: Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor

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About: Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 1973

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1973 (uk) im April 1973 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 1973 (ast) scientific article published on 01 April 1973 (en)
publication date	wds:Q69532767-D5454424-C346-40A0-9E43-62045FED203B
publication date	1973-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q69532767-5F4C3D90-A249-4D56-90FA-6FB05FB72D16
language of work or name	English
cites work	wds:Q69532767-0BB2994D-D002-44D1-9DF0-500C5FEF622F wds:Q69532767-15CC8C86-5B72-4830-B40C-9CA1224C0A45 wds:Q69532767-2B61995C-A17A-4C5D-B343-614B43523BC2 wds:Q69532767-7275A334-587D-4466-B025-B0959BA6C0B8 wds:Q69532767-89179055-FC32-4637-970E-9246ECA8A6D2 wds:Q69532767-A9E28545-E10E-4B0C-904F-FCE6D6B9F6FC wds:Q69532767-FBAD2374-5017-43F3-9EFB-86E404E42CD2
cites work	Hydrogen Exchange in Proteins Primary structure effects on peptide group hydrogen exchange. ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUND The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages The Conformational Properties of the Basic Pancreatic Trypsin-Inhibitor Proton magnetic resonance spectra of proteins in random-coil configurations Pancreatic Trypsin Inhibitor (Kunitz): Part I: Structure and function
author name string	wds:Q69532767-F13918A6-C5E4-441C-B2C7-C33A91E67D3E
author name string	Masson A
rdfs:label	Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (en) Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (nl)
skos:prefLabel	Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (en) Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (nl)
name	Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (en) Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (nl)
author	wds:Q69532767-F86FC87F-C998-4587-95C5-10752D3839DF
author	Kurt Wüthrich
title	wds:Q69532767-038640B1-F5BC-4A26-88DC-AA9A4627AD95
title	Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor (en)
page(s)	wds:Q69532767-73809162-B5D1-4627-BC31-A476C31404CC
page(s)	114-118
instance of	wds:Q69532767-B4AD933C-7C3D-4813-AD16-75132E427756
instance of	scholarly article
PubMed ID	wds:Q69532767-1EC6DA53-35FC-4E31-BAFA-84074938ECB5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4709991
PubMed ID	4709991
published in	wds:Q69532767-D3C854FC-7A4A-431A-B4BA-BD3A3DE86ADB
published in	FEBS Letters
issue	wds:Q69532767-6F5B0008-B42B-4FC2-AF17-B5C8FEBDBB4B
volume	wds:Q69532767-FA23B4FB-2BB4-49C8-87AF-55EE4B05CBF4
issue	1
volume	31
DOI	wds:Q69532767-0BC3D236-8D6E-4858-AB4C-F64071354ABA
DOI	http://dx.doi.org/10.1016/0014-5793(73)80086-9
DOI	10.1016/0014-5793(73)80086-9
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69532767
is cites work of	Hydrogen exchange and the dynamic structure of proteins Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor Experimental studies of protein folding and unfolding Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects Observation of internal motility of proteins by nuclear magnetic resonance in solution The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor Motions in Proteins Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor Mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) Electrophoretic analysis of the unfolding of proteins by urea Dynamic model of globular protein conformations based on NMR studies in solution Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). II. Semi-empirical energy calculations Individual assignments of the methyl resonances in the proton nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor A Comparative Study on the Basic Pancreatic Trypsin Inhibitor and Insulin by the Hydrogen-Exchange Method 1 H NMR titration shifts of amide proton resonances in polypeptide chains Renaturation of the reduced bovine pancreatic trypsin inhibitor Concentration-dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease S A Study of the Lysyl Residues in the Basic Pancreatic Trypsin Inhibitor using 1H Nuclear Magnetic Resonance at 360 MHz A 1H nuclear-magnetic-resonance study of the solution conformation of the isoinhibitor K from Helix pomatia Bicyclic peptides as type I/type II beta-turn scaffolds Nuclear magnetic resonance in protein research Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor Role of the environment in the refolding of reduced pancreatic trypsin inhibitor Proton magnetic resonances in cytochrome b2 core structural similarities with cytochrome b5 1H Nuclear-Magnetic-Resonance Studies of the Porcine-Pancreatic Secretory Trypsin Inhibitor at 270 MHz The charge-relay system of serine proteinases: Proton magnetic resonance titration studies of the four histidines of porcine trypsin p2H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 1438 Hydrogen exchange in RNase A: neutron diffraction study 1H n.m.r. studies of a neurotoxin and a cardiotoxin from Naja mossambica mossambica: amide proton resonances Conformational dynamics of porcine pancreatic colipase: a 360MHz proton nuclear magnetic resonance study Studies on DNA Unwinding. Proton and Phosphorus Nuclear-Magnetic-Resonance Studies of Gene V Protein from Bacteriophage M 13, Interacting with d(pC-G-C-G) Intramolecular Interactions, Enzyme Activity and Models The Influence of Localized Chemical Modifications of the Basic Pancreatic Trypsin Inhibitor on Static and Dynamic Aspects of the Molecular Conformation in Solution 1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by 1H NMR at 360 MHz High field13C NMR studies at 90.5 MHz of the methyl groups in the basic pancreatic trypsin inhibitor

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