(Q28259315)

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Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme

scientific article (publication date: 5 February 1985)

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Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme (English)

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1

M Levitt

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author name string

C Sander

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2

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P S Stern

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3

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language of work or name

English

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publication date

5 February 1985

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published in

Journal of Molecular Biology

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volume

181

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page(s)

423-47

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3

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cites work

Structure of ribonuclease A: results of joint neutron and X-ray refinement at 2.0-A resolution

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

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Dynamic information from protein crystallography. An analysis of temperature factors from refinement of the hen egg-white lysozyme structure

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Consistent Force Field for Calculations of Conformations, Vibrational Spectra, and Enthalpies of Cycloalkane and n‐Alkane Molecules

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Collective variable description of small-amplitude conformational fluctuations in a globular protein

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Protein folding by restrained energy minimization and molecular dynamics

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Low‐frequency Raman spectra of lysozyme

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur

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Automatic identification of secondary structure in globular proteins

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A solution for the best rotation to relate two sets of vectors

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Intramolecular low-frequency vibrations in lysozyme by neutron time-of-flight spectroscopy

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Neutron-scattering spectroscopy of the ?- and ?- forms of poly-L-alanine. Motion of the methyl side chain

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Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

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

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Functional significance of flexibility in proteins

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Fluctuations of an α‐helix

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

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Vibrational frequencies and modes of alpha-helix

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Identifiers

DOI

10.1016/0022-2836(85)90230-X

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

5086378

OpenCitations bibliographic resource ID

5086378

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

5086378

(Q28259315)

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme

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