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With the huge increase in available data on the DNA sequences of proteins, there is a growing need to understand and characterize how proteins fold into their biologically active native states and the basis for the stability of these states. In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating aspects of protein stability and dynamics from knowledge of the structure, for calculating conformational entropy, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches presented include the use of co-solvents, novel applications of hydrogen exchange techniques, temperature-jump methods for looking at folding events, and new strategies for mutagenesis experiments. Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of this complex area by detailing many of the major innovative techniques in use today.
Protein folding. --- Proteins --- Conformation. --- Protein conformation --- Folding of proteins --- Folding --- Conformation --- Biochemistry. --- Biochemistry, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Composition --- Protein folding --- Protein Conformation --- Protein Folding --- Structure-Activity Relationship --- 577.122 --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Proteostasis --- Protein Multimerization --- Intrinsically Disordered Proteins --- Conformation, Protein --- Conformations, Protein --- Protein Conformations --- 577.122 Protein metabolism --- Protein metabolism --- Relationship, Structure-Activity --- Relationships, Structure-Activity --- Structure Activity Relationship --- Structure-Activity Relationships --- chemistry --- PROTEINS --- PROTEIN FOLDING --- CONFORMATION
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Protein Folding --- Proteins --- Protein folding --- Protéines --- physiology --- Congresses. --- Repliement --- Congrès --- Protéines --- Congrès --- Evolution, molecular --- Glass transition --- Protein conformation --- Simulation and modeling, biological
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The relationship between longevity and different traits scored in the Swedish Riding Horse Quality Test (RHQT) was studied to evaluate their use as predictors of survival. Data comprised 1815 Warmblood horses born between 1969 and 1982 that had participated in the RHQT as 4-year-olds. Survival information was obtained via a questionnaire sent to owners of horses that had participated in the RHQT between 1973 and 1986. All phenotypic values of traits scored at 4 years of age were adjusted for the effect of place/year (event). Survival analysis was performed taking into account censoring. Traits having significant effects on longevity were: conformation, legs (included in conformation), orthopaedic status, jumping ability, and the horses' combined classification score for dressage and jumping talents, respectively. Orthopaedic health had the greatest influence on longevity, and demonstrated the importance of judging health traits in young sports horses. The results of this study confirmed that there is a significant phenotypic relationship between many of the RHQT traits and longevity, and thus the possibility of using them as predictors of survival. (C) 2001 Elsevier Science B.V. All rights reserved
Ability. --- Age. --- Analysis. --- Boxes. --- Breeding. --- Classification. --- Conformation. --- Dressage. --- Health. --- Horse. --- Horses. --- Jumping. --- Longevity. --- Quality. --- Questionnaire. --- Survival analysis. --- Survival. --- Test traits. --- Test. --- Time. --- Young.
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Supramolecular chemistry --- Chimie supramoléculaire --- Supramolecular chemistry. --- Chemistry, Physical and theoretical --- Macromolecules --- Macromolecular Systems --- Chemistry --- Molecular Conformation --- Molecular Structure --- Structure, Molecular --- Molecular Structures --- Structures, Molecular --- Models, Molecular --- 3D Molecular Structure --- Configuration, Molecular --- Molecular Structure, Three Dimensional --- Three Dimensional Molecular Structure --- Molecular Configuration --- 3D Molecular Structures --- Configurations, Molecular --- Conformation, Molecular --- Conformations, Molecular --- Molecular Configurations --- Molecular Conformations --- Molecular Structure, 3D --- Molecular Structures, 3D --- Structure, 3D Molecular --- Structures, 3D Molecular --- Macromolecular Substances. --- Chemistry. --- Molecular Conformation. --- Molecular Structure. --- Macromolecular Complexes --- Macromolecular Compounds --- Macromolecular Compounds and Complexes --- Complexes, Macromolecular --- Compounds, Macromolecular --- Substances, Macromolecular --- Nanostructures --- Molecular structure. --- Chimie. --- Structure moléculaire. --- chemistry. --- molecular structure. --- Chemical structure --- Structural bioinformatics --- Physical sciences
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547.964 --- 577.112 --- Proteins --- -biochemie --- proteïnen --- eiwitten --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- 577.112 Proteins --- 547.964 Protein derivatives and decomposition products. Peptones. Polypeptides --- Protein derivatives and decomposition products. Peptones. Polypeptides --- Structure --- -Proteids --- -Protein derivatives and decomposition products. Peptones. Polypeptides --- -547.964 Protein derivatives and decomposition products. Peptones. Polypeptides --- biochemie --- General biophysics --- General biochemistry --- Molecular biology --- Structure. --- Protéines --- Proteins - Structure --- PHOTOSYNTHESIS --- MOLECULAR STRUCTURE --- CONFORMATION --- EVOLUTION, MOLECULAR --- PROTEINS --- PROPERTIES --- STRUCTURES
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