About: Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

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About: Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance Goto Sponge NotDistinct Permalink

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scientific article published on 01 September 1982

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 1982 (uk) im September 1982 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 September 1982 (en) artículu científicu espublizáu en setiembre de 1982 (ast)
publication date	wds:Q72684541-46F8017C-2B53-4897-93DD-6986A66A759A
publication date	1982-09-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q72684541-021CC9DE-F859-49B0-A683-A931DE0D94D9 wds:Q72684541-0B57FEBC-9D7B-4897-9336-135CD6AF9C6F wds:Q72684541-110FBB97-1FF4-4969-A1A9-24A81A3E2941 wds:Q72684541-12907813-0E70-48BB-B1E3-D51E3435EEAA wds:Q72684541-13421354-1E82-4D91-A3F7-BA8F616B8AFD wds:Q72684541-1DBF080A-BDD1-4DDC-B204-99512030F9B9 wds:Q72684541-1ECF3AA7-9B15-4288-8CBF-A6188CE84B79 wds:Q72684541-3368F67C-52FF-4BEA-98FC-E5A732ADE8C1 wds:Q72684541-3B064FB7-19F9-4ABA-90AA-BA130622A4DA wds:Q72684541-550C861F-2DF7-44D9-B29D-44F77218970F wds:Q72684541-55A06CC6-6E5A-483B-8121-68C66F541E81 wds:Q72684541-59E023FA-4A7A-4C7A-8808-52FF5E583853 wds:Q72684541-62C5D1A2-87FB-4F87-9826-1C6220337EAB wds:Q72684541-6443C5F1-EC79-47A2-AC75-F060318BF1EE wds:Q72684541-6557E9C2-5202-42E0-93EB-156A85E491CA wds:Q72684541-8122E507-7A12-42C9-92B4-55E75D9427FA wds:Q72684541-8C7BA112-E99B-4F28-8095-ED7867AC1203 wds:Q72684541-8DB79469-40E5-47BC-8384-3813AEC6D9B5 wds:Q72684541-8E79C837-7AF5-4EBF-80D9-8D1130A3DCE8 wds:Q72684541-9076BD73-946E-4E30-8D1E-4FD8CAF04698 wds:Q72684541-9945DE07-7FEE-4F4C-B229-604FB1875C85 wds:Q72684541-9ED49CB7-E8A8-432E-AC43-DE852EAC7154 wds:Q72684541-AD4B0D2A-54F4-40BB-9431-D1A06FD3C0CC wds:Q72684541-B4B779A7-589E-4D2E-8CD0-D7CF25E36A31 wds:Q72684541-C39059DC-D8A8-4FD5-9398-867F060A56BB wds:Q72684541-CF7E65AA-B023-44C3-8925-78626E570A71 wds:Q72684541-D7B94395-769D-4456-BD3D-AEE8ABB969EF wds:Q72684541-DD200425-647E-46D1-B476-7A2A2EB5488F wds:Q72684541-E15A5613-8E4C-4DB9-9CAB-AE8233BE3AFC wds:Q72684541-E30CC068-7F66-4357-BE89-3EC5A4E0C11A wds:Q72684541-F2F33DB9-496A-4413-A276-0B401EB976F9 wds:Q72684541-F8EB2E4A-7F5C-48C1-9339-784838D84361 wds:Q72684541-FBAF18D3-5748-4804-A61E-421491AFC845
cites work	Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery Hydrogen exchange Hydrogen Exchange in Proteins Primary structure effects on peptide group hydrogen exchange. Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 2. Combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidat The interpretation of protein structures: Estimation of static accessibility Principles of protein-protein recognition Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide The anatomy and taxonomy of protein structure Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance Carboxypeptidase A: a protein and an enzyme. The internal dynamics of globular proteins. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. Two-dimensional spin echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromolecules Studies of J-connectivities and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor Two‐dimensional spectroscopy. Application to nuclear magnetic resonance Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance 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) Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analog Nmr studies of aqueous solutions of tetra and branched peptides. I. Sequence determination of amino-acid residues and the assignment of peptide hydrogen signals Correlations between internal mobility and stability of globular proteins Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea 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
author name string	wds:Q72684541-27B1BE50-2A8E-4619-913E-580826B2BF37
author name string	G Wagner
rdfs:label	Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (en) Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (nl)
skos:prefLabel	Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (en) Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (nl)
name	Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (en) Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (nl)
author	wds:Q72684541-A48C7397-477A-4A18-8603-8D9D3170C092
author	Kurt Wüthrich
title	wds:Q72684541-8222F9B0-7D1A-4D4B-A0E5-0D36D4154475
title	Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (en)
page(s)	wds:Q72684541-7B30A4AB-49CE-4209-81A8-127E1DDAEE15
page(s)	343-361
instance of	wds:Q72684541-9845A2B8-4C49-4F5C-82EE-CE09D3F44EA4
instance of	scholarly article
PubMed ID	wds:Q72684541-C289DE39-0C70-4E3D-AB1F-44035D867F6C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6184480
PubMed ID	6184480
published in	wds:Q72684541-7A6B7F9E-555D-4C27-88CD-7AF524215E4C
published in	Journal of Molecular Biology
issue	wds:Q72684541-167EE940-189A-47DF-8825-7A8C42113BC5
volume	wds:Q72684541-0B5EF52A-C3AF-4567-A12E-2CC1C3AC4475
issue	2
volume	160
DOI	wds:Q72684541-48DFB570-ED3B-42E4-BC1E-5C37D57DB4BD

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