Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized kappa-casein structure

A refined three-dimensional molecular model of kappa-casein has been produced using energy minimization techniques and a Kollman force field on a previously reported predicted three-dimensional structure. This initial model was constructed via molecular modeling techniques from sequence-based second...

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Bibliographic Details
Published in:Journal of dairy science 1993-09, Vol.76 (9), p.2507-2520
Main Authors: Kumosinski, T. F, Brown, E. M, Farrell, H. M., Jr
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Animals
Biological and medical sciences
casein
caseina
caseine
Caseins - chemistry
Cattle
Chemical Phenomena
Chemistry, Physical
Chymosin - metabolism
Computer Simulation
energia
energie
energy
Food industries
Fundamental and applied biological sciences. Psychology
Macromolecular Substances
modele
modelos
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
Sequence Homology, Amino Acid
Spectroscopy, Fourier Transform Infrared
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Summary:A refined three-dimensional molecular model of kappa-casein has been produced using energy minimization techniques and a Kollman force field on a previously reported predicted three-dimensional structure. This initial model was constructed via molecular modeling techniques from sequence-based secondary structural prediction algorithms. Both the initial and refined structures agreed with global secondary structure analysis from vibration spectroscopy. The refined structure contained many of the features of the initial model, including two sets of antiparallel beta-sheet structures containing predominantly hydrophobic side chains, which could form interaction sites with alpha(s1)-casein. Two types of energy-minimized dimer and tetramer models are presented: 1) using Cys as potential intermolecular disulfide binding sites and 2) using the two sheets as possible hydrophobic self-association sites, without Cys interactions. All structures yielded good stabilization energies and are in agreement with chemical, biochemical, and physical chemical results obtained for kappa-casein.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(93)77586-4