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Structure and Mechanism in Protein Science : a guide to enzyme catalysis and protein folding

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TLDR
The three-dimensional structure of proteins chemical catalysis, kinetics measurement and magnitude of enzymatic rate constants, and the use of binding energy in catalysis specificity and editing mechanisms are studied.
Abstract
The three-dimensional structure of proteins chemical catalysis the basic equations of enzyme kinetics measurement and magnitude of enzymatic rate constants the pH dependence of enzyme catalysis practical kinetics detection of intermediaries in reactions by kinetics stereochemistry of enzymic reactions active-site-directed and enzyme-activated irreversible inhibitors - affinity labels and suicide inhibitors conformational change, allosteric regulation, motors and work forces between molecules, and enzyme-substrate binding energies enzyme-substrate complementarity and the use of binding energy in catalysis specificity and editing mechanisms recombinant DNA technology case studies of enzyme structure and mechanism protein engineering protein stability kinetics of protein folding folding pathways and energy landscapes.

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Journal ArticleDOI

Protein folding and misfolding

TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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Improving enzymes by using them in organic solvents

TL;DR: The technological utility of enzymes can be enhanced greatly by using them in organic solvents rather than their natural aqueous reaction media, and they have found numerous potential applications, some of which are already commercialized.
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The amyloid state and its association with protein misfolding diseases

TL;DR: The ability to form the amyloid state is more general than previously imagined, and its study can provide unique insights into the nature of the functional forms of peptides and proteins, as well as understanding the means by which protein homeostasis can be maintained and protein metastasis avoided.
Journal ArticleDOI

Glycosyltransferases: structures, functions, and mechanisms.

TL;DR: The expected two-step double-displacement mechanism is rendered less likely by the lack of conserved architecture in the region where a catalytic nucleophile would be expected, and a mechanism involving a short-lived oxocarbenium ion intermediate now seems the most likely, with the leaving phosphate serving as the base.
Journal ArticleDOI

Solvent Mediated Interactions in the Structure of the Nucleosome Core Particle at 1.9 Å Resolution

TL;DR: A single-base-pair increase in DNA length over that used previously results in substantially improved clarity of the electron density and accuracy for the histone protein and DNA atomic coordinates, and reduced disorder has allowed for the first time extensive modeling of water molecules and ions.
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