Literature DB >> 5167778

The conformational properties of the basic pancreatic trypsin-inhibitor.

J P Vincent, R Chicheportiche, M Lazdunski.   

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Year:  1971        PMID: 5167778     DOI: 10.1111/j.1432-1033.1971.tb01634.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


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  7 in total

1.  1H Nmr studies at 360 MHz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI).

Authors:  A De Marco; H Tschesche; G Wagner; K Wüthrich
Journal:  Biophys Struct Mech       Date:  1977-09-28

2.  Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). I. 1H NMR studies.

Authors:  G Wagner; A DeMarco; K Wüthrich
Journal:  Biophys Struct Mech       Date:  1976-08-23

3.  [Nuclear magnetic resonance spectroscopy in biological research].

Authors:  K Wüthrich
Journal:  Naturwissenschaften       Date:  1973-05

4.  Minimal effects of macromolecular crowding on an intrinsically disordered protein: a small-angle neutron scattering study.

Authors:  David P Goldenberg; Brian Argyle
Journal:  Biophys J       Date:  2014-02-18       Impact factor: 4.033

5.  Self crowding of globular proteins studied by small-angle x-ray scattering.

Authors:  David P Goldenberg; Brian Argyle
Journal:  Biophys J       Date:  2014-02-18       Impact factor: 4.033

6.  Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor.

Authors:  C K Woodward; B D Hilton
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

7.  BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path.

Authors:  Reem Mousa; Shifra Lansky; Gil Shoham; Norman Metanis
Journal:  Chem Sci       Date:  2018-05-02       Impact factor: 9.825

  7 in total

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