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The role of an L-leucine residue on the conformations of glycyl-L-leucine oligomers and its N- or C-terminal dependence: infrared absorption and Raman scattering studies.
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Local structure involving histidine-12 in reduced S-sulfonated ribonuclease A detected by proton NMR spectroscopy under folding conditions.
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The influence of short-range interactions on protein onformation. II. A model for predicting the alpha-helical regions of proteins.
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Analysis of the code relating sequence to conformation in globular proteins. An informational analysis of the role of the residue in determining the conformation of its neighbours in the primary sequence.
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Three-dimensional structure of tosyl-alpha-chymotrypsin.
Nature. 1967 May 13;214(5089):652-6. doi: 10.1038/214652a0.
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Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.
Biophys J. 1967 Mar;7(2):121-35. doi: 10.1016/S0006-3495(67)86579-2.
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Conformation of analysis of macromolecules. IV. Helical structures of poly-L-alanine, poly-L-valine, poly-beta-methyl-L-aspartate, poly-gamma-methyl-L-glutamate, and poly-L-tyrosine.
J Chem Phys. 1967 Jun 1;46(11):4410-26. doi: 10.1063/1.1840561.
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Tertiary structure of ribonuclease.
Nature. 1967 Mar 4;213(5079):862-5. doi: 10.1038/213862a0.
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Recognition of alpha-helical segments in proteins of known primary structure.
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Correlation between the distribution of amino acids and alpha helices.
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Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
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The influence of amino-acid sequence on protein structure.
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Prediction of alpha-helical regions in proteins of known sequence.
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Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide.
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