Thermodynamics, Kinetics and Landscapes in Alpha-lytic Protease PDF Download

Author: Sheila Jaswal
Publisher:
ISBN:
Category :
Languages : en
Pages : 324

View

Book Description

Author: Stephanie Marie Truhlar
Publisher:
ISBN:
Category :
Languages : en
Pages : 308

View

Book Description

Author: Tony R. Obalinsky
Publisher: Nova Publishers
ISBN: 9781594548352
Category : Protein folding
Languages : en
Pages : 294

View

Book Description
Proteins are one of the most basic components of all living cells and therefore serve a vital purpose in the cells of animals, plants and bacteria. They are comprised of chains of amino acids, which are held together by ribosome. These chains have many different patterns, which are known as `folds.' These folds are complicated, and therefore susceptible to irregularities that are known to be the source of many diseases. Cystic fibrosis, mad cow disease, Alzheimer's disease, emphysema and others are all initiated by improper protein folds. It is clear that, improving our understanding of protein folding is a key to fighting these diseases. This book presents recently performed research from around the world on this important subject.

Author: Angel L. Pey
Publisher: Academic Press
ISBN: 0128191333
Category : Science
Languages : en
Pages : 450

View

Book Description
Protein Homeostasis Diseases: Mechanisms and Novel Therapies offers an interdisciplinary examination of the fundamental aspects, biochemistry and molecular biology of protein homeostasis disease, including the use of natural and pharmacological small molecules to treat common and rare protein homeostasis disorders. Contributions from international experts discuss the biochemical and genetic components of protein homeostasis disorders, the mechanisms by which genetic variants may cause loss-of-function and gain-of-toxic-function, and how natural ligands can restore protein function and homeostasis in genetic diseases. Applied chapters provide guidance on employing high throughput sequencing and screening methodologies to develop pharmacological chaperones and repurpose approved drugs to treat protein homeostasis disorders. Provides an interdisciplinary examination of protein homeostasis disorders, with an emphasis on treatment strategies employing small natural and pharmacological ligands Offers applied approaches in employing high throughput sequencing and screening to develop pharmacological chaperones to treat protein homeostasis disease Gathers expertise from a range of international chapter authors who work across various biological methods and disease specific disciplines of relevance

Author: Erin Lynn Cunningham
Publisher:
ISBN:
Category :
Languages : en
Pages : 288

View

Book Description

Author: Amit Kessel
Publisher: CRC Press
ISBN: 1498747213
Category : Computers
Languages : en
Pages : 1489

View

Book Description
Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the structure, function, and motion of proteins for students, faculty, and researchers at all levels. The book covers proteins and enzymes across a wide range of contexts and applications, including medical disorders, drugs, toxins, chemical warfare, and animal behavior. Each chapter includes a Summary, Exercies, and References. New features in the thoroughly-updated second edition include: A brand-new chapter on enzymatic catalysis, describing enzyme biochemistry, classification, kinetics, thermodynamics, mechanisms, and applications in medicine and other industries. These are accompanied by multiple animations of biochemical reactions and mechanisms, accessible via embedded QR codes (which can be viewed by smartphones) An in-depth discussion of G-protein-coupled receptors (GPCRs) A wider-scale description of biochemical and biophysical methods for studying proteins, including fully accessible internet-based resources, such as databases and algorithms Animations of protein dynamics and conformational changes, accessible via embedded QR codes Additional features Extensive discussion of the energetics of protein folding, stability and interactions A comprehensive view of membrane proteins, with emphasis on structure-function relationship Coverage of intrinsically unstructured proteins, providing a complete, realistic view of the proteome and its underlying functions Exploration of industrial applications of protein engineering and rational drug design Each chapter includes a Summary, Exercies, and References Approximately 300 color images Downloadable solutions manual available at www.crcpress.com For more information, including all presentations, tables, animations, and exercises, as well as a complete teaching course on proteins' structure and function, please visit the author's website: http://ibis.tau.ac.il/wiki/nir_bental/index.php/Introduction_to_Proteins_Book. Praise for the first edition "This book captures, in a very accessible way, a growing body of literature on the structure, function and motion of proteins. This is a superb publication that would be very useful to undergraduates, graduate students, postdoctoral researchers, and instructors involved in structural biology or biophysics courses or in research on protein structure-function relationships." --David Sheehan, ChemBioChem, 2011 "Introduction to Proteins is an excellent, state-of-the-art choice for students, faculty, or researchers needing a monograph on protein structure. This is an immensely informative, thoroughly researched, up-to-date text, with broad coverage and remarkable depth. Introduction to Proteins would provide an excellent basis for an upper-level or graduate course on protein structure, and a valuable addition to the libraries of professionals interested in this centrally important field." --Eric Martz, Biochemistry and Molecular Biology Education, 2012

Author: Alan J. Barrett
Publisher: Academic Press
ISBN: 0123822203
Category : Science
Languages : en
Pages : 4097

View

Book Description
Extensively revised and updated, the new edition of the highly regarded Handbook of Proteolytic Enzymes is an essential reference for biochemists, biotechnologists and molecular biologists. Edited by world-renowned experts in the field, this comprehensive work provides detailed information on all known proteolytic enzymes to date. This two-volume set unveils new developments on proteolytic enzymes which are being investigatedin pharmaceutical research for such diseases as HIV, Hepatitis C, and the common cold. Volume I covers aspartic and metallo petidases while Volume II examines peptidases of cysteine, serine, threonine and unknown catalytic type. A CD-ROM accompanies the book containing fully searchable text, specialised scissile bond searches, 3-D color structures and much more. The only comprehensive book on proteolytic enzymes Includes 671 chapters, each written by experts in their field, on proteolytic enzymes from all groups of living organisms and the viruses, including those that are currently major targets of pharmaceutical research Accompanying CD-ROM provides fully searchable text, 2D structures of peptidases in color and links directly to PubMed and MEROPS databases Each chapter describes in detail the enzyme name, its history, activity and specificity, structural chemistry, preparation, biological aspects and distinguishing features Over 1000 peptidases included

Author: José Luis R. Arrondo
Publisher: Springer Science & Business Media
ISBN: 3540307869
Category : Science
Languages : en
Pages : 290

View

Book Description
Technical advancements are basic elements in our life. In biophysical studies, new applications and improvements in well-established techniques are being implemented every day. This book deals with advancements produced not only from a technical point of view, but also from new approaches that are being taken in the study of biophysical samples, such as nanotechniques or single-cell measurements. This book constitutes a privileged observatory for reviewing novel applications of biophysical techniques that can help the reader enter an area where the technology is progressing quickly and where a comprehensive explanation is not always to be found.

Author: Cynthia Nichole Fuhrmann
Publisher:
ISBN:
Category :
Languages : en
Pages : 474

View

Book Description
For many decades, [alpha]-lytic protease ([alpha]LP), an extracellular bacterial protease secreted by Lysobacter enzymogenes , has served as a model in both mechanistic and structural studies for chymotrypsin-like serine proteases. In order to address questions regarding the catalytic mechanism of serine proteases, I determined three structures of [alpha]LP at ultra-high resolution: (1) the free enzyme at its active pH ([alpha]LP pH 8 ; 0.83Å resolution), (2) [alpha]LP at pH5 ([alpha]LP pH 5 ; 0.82Å resolution), and (3) [alpha]LP bound to a peptidyl boronic acid inhibitor, McOSuc-Ala-Ala-Pro-boroVal ([alpha]LP+boroVal(gol); 0.90Å resolution). The latter two structures provided analogs to the transition states of the catalytic reaction. The unexpected covalent binding of a glycerol molecule to the tetrahedral boronate in ([alpha]LP+boroVal(gol); provided the most accurate and highly-resolved model of the tetrahedral intermediate for acylation (TI 1) determined to date. Structure-specific radiation damage was apparent in electron density for these structures, and special data collection techniques were used to minimize radiation damage observed at the Ser195-boronic acid adduct. A comparison of all three structures elucidated the structural changes that occur during the first step of the catalytic reaction (ES [arrow right] TI 1 ). We propose that upon deprotonation of His57, Ser195 undergoes a conformational change that is responsible for preventing the TI 1 [arrow right] ES back-reaction. Based on precise atomic positions obtained at sub-Ångstrom resolution, we have concluded that the His57...Asp102 interaction is a standard ionic hydrogen bond in both the free enzyme and the acylation transition state, and not a low-barrier hydrogen bond as had been previously debated. Instead, I propose that transition state stabilization by chymotrypsin-like serine proteases is achieved through a network of optimized hydrogen bonds that position the catalytic triad and stabilize the Ser195-substrate tetrahedral adduct. In particular, I identified a short, ionic hydrogen bond between His57 and the amide of the substrate leaving group that may play the primary role in catalyzing the second step of the acylation reaction. A surprising outcome from these studies was the discovery of a site of conformational strain that appears to be evolutionarily linked to [alpha]LP's kinetic stability. Distortion of Phe228, a conserved residue in the protein core, is estimated to account for ~4 kcal/mol in conformational energy. The rearrangement and subsequent distortion of Phe228 by co-evolved residues surrounding it supports the hypothesis that tight packing in [alpha]LP is a key component of [alpha]LP's folding energy landscape. Subsequent mutational studies support this hypothesis, confirming our discovery of the first known functionally-relevant distortion.

Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 2452

View

Book Description
Vols. for 1963- include as pt. 2 of the Jan. issue: Medical subject headings.