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Prediction of protein structure from ideal forms

Proteins: Structure, Function, and Bioinformatics, 2008
AbstractFor many years it has been accepted that the sequence of a protein can specify its three‐dimensional structure. However, there has been limited progress in explaining how the sequence dictates its fold and no attempt to do this computationally without the use of specific structural data has ever succeeded for any protein larger than 100 ...
William R, Taylor   +6 more
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Determination of ideal protein ratios in growing pullets

Animal Feed Science and Technology, 2022
2022
Soares, Letícia   +7 more
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Strong non-ideality effects at low protein concentrations: considerations for elongated proteins

European Biophysics Journal, 2022
AbstractA recent investigation was aimed at obtaining structural information on a highly extended protein via SEC-MALS-SAXS. Significantly broadened elution peaks were observed, reminiscent of a phenomenon known as viscous fingering. This phenomenon is usually observed above 50 mg/mL for proteins like bovine serum albumin (BSA).
Alexander E. Yarawsky   +3 more
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Is lysozyme really the ideal model protein?

Journal of Crystal Growth, 2001
A series of potential heterogeneous nucleants were added to metastable solutions of lysozyme and of four other model proteins, as well as to a few target proteins. Some of the substances markedly affected the nucleation of lysozyme crystals, but did not influence the other proteins.
Naomi E Chayen, Emmanuel Saridakis
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Polyprotein of GB1 is an ideal artificial elastomeric protein

Nature Materials, 2007
Naturally occurring elastomeric proteins function as molecular springs in their biological settings and show mechanical properties that underlie the elasticity of natural adhesives, cell adhesion proteins and muscle proteins. Constantly subject to repeated stretching-relaxation cycles, many elastomeric proteins demonstrate remarkable consistency and ...
Yi, Cao, Hongbin, Li
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In search of the ideal protein sequence

"Protein Engineering, Design and Selection", 1995
The inverse of a folding problem is to find the ideal sequence that folds into a particular protein structure. This problem has been addressed using the topology fingerprint-based threading algorithm, capable of calculating a score (energy) of an arbitrary sequence-structure pair.
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