(Q52590877)

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Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.

scientific article published in August 1987

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Europe PubMed Central

PubMed publication ID

4 May 2018

http://europepmc.org/abstract/MED/2445992

Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 May 2018

http://europepmc.org/abstract/MED/2445992

protein folding

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Wüthrich K

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4 May 2018

http://europepmc.org/abstract/MED/2445992

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Wagner G

1

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4 May 2018

http://europepmc.org/abstract/MED/2445992

Braun W

2

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4 May 2018

http://europepmc.org/abstract/MED/2445992

Havel TF

3

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4 May 2018

http://europepmc.org/abstract/MED/2445992

Schaumann T

4

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4 May 2018

http://europepmc.org/abstract/MED/2445992

Go N

5

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4 May 2018

http://europepmc.org/abstract/MED/2445992

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publication date

1 August 1987

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4 May 2018

http://europepmc.org/abstract/MED/2445992

language of work

Journal of Molecular Biology

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4 May 2018

http://europepmc.org/abstract/MED/2445992

196

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4 May 2018

http://europepmc.org/abstract/MED/2445992

3

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4 May 2018

http://europepmc.org/abstract/MED/2445992

611-639

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Europe PubMed Central

PubMed publication ID

4 May 2018

http://europepmc.org/abstract/MED/2445992

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.

1 reference

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor

1 reference

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NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor

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Pancreatic trypsin inhibitor. A new crystal form and its analysis

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The internal dynamics of globular proteins.

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The Protein Data Bank: a computer-based archival file for macromolecular structures

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Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat

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Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II

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Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance

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Rapid calculation of first and second derivatives of conformational energy with respect to dihedral angles for proteins general recurrent equations

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Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

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How alike are the shapes of two random chains?

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Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance

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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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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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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

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Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure

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An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution

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Representation of short and long-range handedness in protein structures by signed distance maps

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Combined use of proton-proton overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon

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A Method of Rapid Calculation of a Second Derivative Matrix of Conformational Energy for Large Molecules

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Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm

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Approach to the tertiary structure of globular proteins

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10.1016/0022-2836(87)90037-4

1 reference

Europe PubMed Central

PubMed publication ID

4 May 2018

http://europepmc.org/abstract/MED/2445992

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 May 2018

http://europepmc.org/abstract/MED/2445992

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