(Q57000556)

English

Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison

scholarly article by Axel T. Brünger published in January 1988

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scholarly article

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title

Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison (English)

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2

Martin Karplus

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author name string

Axel T. Brünger

series ordinal

1

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language of work or name

English

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publication date

1988

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published in

Proteins

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volume

4

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issue

2

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page(s)

148-156

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cites work

Comparison of simple potential functions for simulating liquid water

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Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin

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Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique.

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A new force field for molecular mechanical simulation of nucleic acids and proteins

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Molecular dynamics of native protein. I. Computer simulation of trajectories

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Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

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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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An all atom force field for simulations of proteins and nucleic acids

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Active site of RNase: neutron diffraction study of a complex with uridine vanadate, a transition-state analog

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Molecular dynamics of myoglobin at 298 degrees K. Results from a 300-ps computer simulation

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Active site dynamics of ribonuclease

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Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

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Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor

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Conformation of amino acid side-chains in proteins

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Restart procedures for the conjugate gradient method

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Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor

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Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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Improved simulation of liquid water by molecular dynamics

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Molecular dynamics simulations of native and substrate-bound lysozyme. A study of the average structures and atomic fluctuations

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Identifiers

DOI

10.1002/PROT.340040208

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PubMed publication ID

3227015

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(Q57000556)

Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison

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