The Significance of Beta-72 Asparagine Methylation in C-Phy C Ocy Anin

Total Page:16

File Type:pdf, Size:1020Kb

The Significance of Beta-72 Asparagine Methylation in C-Phy C Ocy Anin Louisiana State University LSU Digital Commons LSU Historical Dissertations and Theses Graduate School 1993 The iS gnificance of Beta-72 Asparagine Methylation in C-Phycocyanin. Beth Ann Thomas Louisiana State University and Agricultural & Mechanical College Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_disstheses Recommended Citation Thomas, Beth Ann, "The iS gnificance of Beta-72 Asparagine Methylation in C-Phycocyanin." (1993). LSU Historical Dissertations and Theses. 5676. https://digitalcommons.lsu.edu/gradschool_disstheses/5676 This Dissertation is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Historical Dissertations and Theses by an authorized administrator of LSU Digital Commons. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand corner and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book. Photographs included in the original manuscript have been reproduced xerographically in this copy. Higher quality 6" x 9" black and white photographic prints are available for any photographs or illustrations appearing in this copy for an additional charge. Contact UMI directly to order. University Microfilms International A Bell & Howell Information Company 300 North Zeeb Road. Ann Arbor. Ml 48106-1346 USA 313/761-4700 800/521-0600 Order Number 9419930 The significance of beta-72 asparagine methylation in C-phy c ocy anin Thomas, Beth Ann, Ph.D. The Louisiana State University and Agricultural and Mechanical Col., 1993 UMI 300 N. Zeeb Rd. Ann Arbor, Ml 48106 THE SIGNIFICANCE OF BETA-72 ASPARAGINE METHYLATION IN C-PHYCOCYANIN A Dissertation Submitted to the Graduate Faculty of the Louisiana State University and Agricultural and Mechanical College in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Department of Biochemistry by Beth Ann Thomas B.S., Louisiana State University, 1988 December 1993 Acknowledgements I would like to thank my thesis advisor, Professor Alan Klotz, for his learned and astute guidance in the laboratory. He never ceased to believe in me and my abilities and very patiently taught me the workings of biochemistiy and in particular, protein chemistry. I owe him a great deal of gratitude for his patience and understanding, and his neverending and delightful sense of humor. I am also greatly indebted to Professor Jeff Nelson, who patiently taught me NMR spectroscopy and molecular mechanics/dynamics methodologies (even at 4 in the afternoon). It is obvious from the results in this document that Jeff provided a great deal of assistance with CHARMM and manipulation of NMR pulse routines. I also greatly appreciate the assistance of Professor Terry Bricker in the photosynthetic characterizations of the methylase-minus mutants; I value his enthusiasm for my thesis project. I would also like to thank the other members of my committee who were valuable consultants: Professor George Stanley, Professor Simon Chang and Professor Ezzat Younathan. I have many wonderful friends at Chapel of the Cross Lutheran Church including Virginia Simoneaux, Dick Felder, Mike Lewis, John Roth, Gary Peterson, Audra Gossett and many others; I thank them for the continual interest in my project and the enormous amounts of emotional and spiritual support. Finally, I thank my parents for their constant financial support throughout graduate school and for the home-cooked meals provided to me during the last few months of graduate school. Table of Contents Acknowledgements .............................................................................................. ii List of Tables .................................................................................................... vi List of Figures ................................................................................................ viii Abbreviations and Trivial Names ................................................................. x A bstract................................................................................................................. xii Chapter 1. Introduction ................................................................................. 1 I. Post-Translational Protein Modifications ....................................... 1 II. Light-Harvesting/Light Reactions of Photosynthesis ...................... 7 III. Light-Harvesting of Antennae of Cyanobacteria ......................... 11 IV. NMA and its Relationship to C-Phycocyanin ............................... 18 V. Scope of Thesis Research ........................................................... 29 Chapter 2. Detection of Methylated Asparagine and Glutamine Residues in Polypeptides ............................................................. 32 I. Introduction ..................................................................................... 32 II. Materials and Methods ................................................................ 33 A. Chemicals............................................................................... 33 B. Sequencing of Peptides containing y-N-Methylasparagine 33 C. Preparation of O- and N-Methyl Amino Acid Derivatives 34 D. Acid Hydrolysis ................................................................... 35 E. Amino Acid Analysis ............................................................. 35 F. Preparation of PTH Derivatives ........................................... 35 G. NMR Analysis ................................... 36 H. Mass Spectrometry ............................................................... 36 III. Results and Discussion ............................................................ 37 Chapter 3. Post-Translational Methylation of Phycobilisomes and Oxygen Evolution Efficiency in Cyanobacteria ....................... 51 I. Introduction ................................... 51 II. Materials and Methods ............................................................... 53 A. Strains and Growth Conditions ............................................ 53 B. Oxygen Evolution Measurements ......................................... 54 C. Statistical Analysis of Quantum Yield Data ........................... 55 D. Stoichiometry od Asparagine Methylation .............................. 56 E. Growth Competition Experiments ......................................... 57 III. Results and Discussion ............................................................ 59 A. Asparagine Methylation ........................................................ 61 B. Effect of Asparagine Methylation on Photosynthetic Rates ..................................................................... 63 C. Growth Competition Experiments ......................................... 72 Chapter 4. Characterization of p-72 Site-Specific Mutants in C-Phycocyanin ................................................................................ 82 I. Introduction ...................................................................................... 82 I. M ethods ............................................................................................ 83 A. Mutant Construction ............................................................. 83 B. Strains and Culture Conditions ........................................... 86 C. Phycocyanin Isolation .......................................................... 87 D. Phycobilisome Isolation ....................................................... 88 E. Isoelectric Focusing .............................................................. 89 F. Glutamine Methylation Analysis .......................................... 90 G. Steady-State Oxygen Evolution Experiments ........................ 91 H. Absorbance Spectroscopy ..................................................... 91 I. Fluorescence Spectroscopy .................................................. 92 J. Molecular Mechanics/Dynamics ............................................ 96 II. Results and Discussion ................................................................ 99 A. Characterization of p-72 Mutations ....................................... 99 B. Isoelectric Focusing ............................................................. 103 C. Radiolabel Analysis of Site-Directed Mutants ....................... 108 D. Characterization of Site-Directed Mutants by Oxygen Evolution ............................................................... 115 E. Characterization of Wild-type and Mutant C-Phycocyanins 119 F. Wild-type and Mutant Phycobilisome Characterization 126 G. Time-Resolved
Recommended publications
  • THE THICKNESSES of HEMOGLOBIN and BOVINE SERUM ALBUMIN MOLECULES AS UNIMOLECULAR LA YERS AD- SORBED ONTO FILMS of BARIUM STEARATE* by ALBERT A
    518 BIOCHEMISTRY: A. A. FISK PROC. N. A. S. THE THICKNESSES OF HEMOGLOBIN AND BOVINE SERUM ALBUMIN MOLECULES AS UNIMOLECULAR LA YERS AD- SORBED ONTO FILMS OF BARIUM STEARATE* By ALBERT A. FIsKt GATES AND CRELLIN LABORATORIES OF CHEMISTRY, CALIFORNIA INSTITUTE OF TECHNOLOGY, PASADENA 4, CALIFORNIAt Communicated by Linus Pauling, July 17, 1950 The following work, which describes a method of measuring one dimen- sion of some protein molecules, is based on the determination of the apparent thickness of a unimolecular layer of globular protein molecules adsorbed from solution onto a metallic slide covered with an optical gauge of barium stearate. Langmuirl' 2 and Rothen3 have published a few results obtained by such a technique, but have not exploited the method thoroughly. A complete set of experimental data has been obtained by Clowes4 on insulin and protamine. He studied the effects of pH and time of exposure on the thickness of layers of protamine and insulin adsorbed onto slides covered with barium stearate and conditioned with uranyl acetate. He found that the pH was responsible for large variations in the thickness of the adsorbed layers and that the thickness of insulin layers adsorbed onto a protamine base was dependent on the concentration of the insulin. Since Clowes found thicknesses as high as 100 A. for protamine and 400 A. for insulin, he was without doubt usually dealing with multi- layers. Experimental.-The apparent thickness of a protein layer is measured with an optical instrument called the ellipsometer by Rothen,5-7 who has given a complete description of its design and optics and has calculated its sensitivity as 0.3 A.
    [Show full text]
  • Flowering Buds of Globular Proteins: Transpiring Simplicity of Protein Organization
    Comparative and Functional Genomics Comp Funct Genom 2002; 3: 525–534. Published online in Wiley InterScience (www.interscience.wiley.com). DOI: 10.1002/cfg.223 Conference Review Flowering buds of globular proteins: transpiring simplicity of protein organization Igor N. Berezovsky1 and Edward N. Trifonov2* 1 Department of Structural Biology, The Weizmann Institute of Science, PO Box 26, Rehovot 76100, Israel 2 Genome Diversity Centre, Institute of Evolution, University of Haifa, Haifa 31905, Israel *Correspondence to: Abstract Edward N. Trifonov, Genome Diversity Centre, Institute of Structural and functional complexity of proteins is dramatically reduced to a simple Evolution, University of Haifa, linear picture when the laws of polymer physics are considered. A basic unit of the Haifa 31905, Israel. protein structure is a nearly standard closed loop of 25–35 amino acid residues, and E-mail: every globular protein is built of consecutively connected closed loops. The physical [email protected] necessity of the closed loops had been apparently imposed on the early stages of protein evolution. Indeed, the most frequent prototype sequence motifs in prokaryotic proteins have the same sequence size, and their high match representatives are found as closed loops in crystallized proteins. Thus, the linear organization of the closed loop elements is a quintessence of protein evolution, structure and folding. Copyright 2002 John Wiley & Sons, Ltd. Received: 31 August 2002 Keywords: loop closure; prototype elements; protein structure; protein folding; Accepted: 14 October 2002 protein evolution; protein design; protein classification Introduction and the probability of the loop ends occurring in the vicinity of one another. The loop closure fortified One fundamental property of the polypeptide chain by the interactions between amino acid residues at is its ability to return to itself with the formation the ends of the loops provides an important degree of closed loops.
    [Show full text]
  • Proteasome System of Protein Degradation and Processing
    ISSN 0006-2979, Biochemistry (Moscow), 2009, Vol. 74, No. 13, pp. 1411-1442. © Pleiades Publishing, Ltd., 2009. Original Russian Text © A. V. Sorokin, E. R. Kim, L. P. Ovchinnikov, 2009, published in Uspekhi Biologicheskoi Khimii, 2009, Vol. 49, pp. 3-76. REVIEW Proteasome System of Protein Degradation and Processing A. V. Sorokin*, E. R. Kim, and L. P. Ovchinnikov Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: [email protected]; [email protected] Received February 5, 2009 Abstract—In eukaryotic cells, degradation of most intracellular proteins is realized by proteasomes. The substrates for pro- teolysis are selected by the fact that the gate to the proteolytic chamber of the proteasome is usually closed, and only pro- teins carrying a special “label” can get into it. A polyubiquitin chain plays the role of the “label”: degradation affects pro- teins conjugated with a ubiquitin (Ub) chain that consists at minimum of four molecules. Upon entering the proteasome channel, the polypeptide chain of the protein unfolds and stretches along it, being hydrolyzed to short peptides. Ubiquitin per se does not get into the proteasome, but, after destruction of the “labeled” molecule, it is released and labels another molecule. This process has been named “Ub-dependent protein degradation”. In this review we systematize current data on the Ub–proteasome system, describe in detail proteasome structure, the ubiquitination system, and the classical ATP/Ub- dependent mechanism of protein degradation, as well as try to focus readers’ attention on the existence of alternative mech- anisms of proteasomal degradation and processing of proteins.
    [Show full text]
  • Folding Units in Globular Proteins (Protein Folding/Domains/Folding Intermediates/Structural Hierarchy/Protein Structure) ARTHUR M
    Proc. NatL Acad. Sci. USA Vol. 78, No. 7, pp. 4304-4308, July 1981 Biochemistry Folding units in globular proteins (protein folding/domains/folding intermediates/structural hierarchy/protein structure) ARTHUR M. LESK* AND GEORGE D. ROSE#T *Fairleigh Dickinson- University, Teaneck, New Jersey 07666; and tDepartment of Biologial Chemistry, The Milton S. Hershey Medical Center, The Pennsylvania State University, Hershey, Per'nsykania 17033 Communicated by Charles Tanford, April 20, 1981 ABSTRACT We presenta method toidentify all compact, con- (ii) Analysis of protein structures elucidated by x-ray crys- tiguous-chain, structural units in a globular protein from x-ray tallography showed that protein molecules can be dissected into coordinates. These units are then used to describe a complete set a succession of spatially compact pieces of graduated size (4). of hierarchic folding pathways for the molecule. Our analysis Each of these elements is formed from a contiguous stretch of shows that the larger units are combinations ofsmaller units, giv- the polypeptide chain. A related analysis was reported by Crip- ing rise to a structural hierarchy ranging from the whole protein pen (5). The spatial compartmentation oflinear segments, seen monomer through supersecondary structures down to individual in the final structure, is likely to be a helices and strands. It turns out that there is more than one way feature of intermediate to assemble the protein by self-association of its compact units. folding stages as well. Otherwise, mixing of chain segments However, the number ofpossible pathways is small-small enough occurring during intermediate stages would have to be followed to be exhaustively explored by a computer program.
    [Show full text]
  • Using Small Globular Proteins to Study Folding Stability and Aggregation
    Using Small Globular Proteins to Study Folding Stability and Aggregation Virginia Castillo Cano September 2012 Universitat Autònoma de Barcelona Departament de Bioquímica i Biologia Molecular Institut de Biotecnologia i de Biomedicina Using Small Globular Proteins to Study Folding Stability and Aggregation Doctoral thesis presented by Virginia Castillo Cano for the degree of PhD in Biochemistry, Molecular Biology and Biomedicine from the University Autonomous of Barcelona. Thesis performed in the Department of Biochemistry and Molecular Biology, and Institute of Biotechnology and Biomedicine, supervised by Dr. Salvador Ventura Zamora. Virginia Castillo Cano Salvador Ventura aZamor Cerdanyola del Vallès, September 2012 SUMMARY SUMMARY The purpose of the thesis entitled “Using small globular proteins to study folding stability and aggregation” is to contribute to understand how globular proteins fold into their native, functional structures or, alternatively, misfold and aggregate into toxic assemblies. Protein misfolding diseases include an important number of human disorders such as Parkinson’s and Alzheimer’s disease, which are related to conformational changes from soluble non‐toxic to aggregated toxic species. Moreover, the over‐expression of recombinant proteins usually leads to the accumulation of protein aggregates, being a major bottleneck in several biotechnological processes. Hence, the development of strategies to diminish or avoid these taberran reactions has become an important issue in both biomedical and biotechnological industries. In the present thesis we have used a battery of biophysical and computational techniques to analyze the folding, conformational stability and aggregation propensity of several globular proteins. The combination of experimental (in vivo and in vitro) and bioinformatic approaches has provided insights into the intrinsic and structural properties, including the presence of disulfide bonds and the quaternary structure, that modulate these processes under physiological conditions.
    [Show full text]
  • Albumin Nanovectors in Cancer Therapy and Imaging
    Review Albumin Nanovectors in Cancer Therapy and Imaging Alessandro Parodi 1,*, Jiaxing Miao 2, Surinder M. Soond 1, Magdalena Rudzińska 1 and Andrey A. Zamyatnin Jr. 1,3,* 1 Institute of Molecular Medicine, Sechenov First Moscow State Medical University, 119991, Moscow, Russia 2 Ohio State University, 410 W 10th Ave. Columbus, 43210, Ohio, USA; [email protected] (S.M.S.); [email protected] (M.R.) 3 Belozersky Institute of Physico‐Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia; [email protected] * Correspondence: [email protected] (A.P.); [email protected] (A.A.Z.Jr.) Received: 24 April 2019; Accepted: 31 May 2019; Published: 5 June 2019 Abstract: Albumin nanovectors represent one of the most promising carriers recently generated because of the cost‐effectiveness of their fabrication, biocompatibility, safety, and versatility in delivering hydrophilic and hydrophobic therapeutics and diagnostic agents. In this review, we describe and discuss the recent advances in how this technology has been harnessed for drug delivery in cancer, evaluating the commonly used synthesis protocols and considering the key factors that determine the biological transport and the effectiveness of such technology. With this in mind, we highlight how clinical and experimental albumin‐based delivery nanoplatforms may be designed for tackling tumor progression or improving the currently established diagnostic procedures. Keywords: albumin; nanomedicine; drug delivery; cancer 1. Introduction During the last decades, a large variety of carriers was generated from different organic and inorganic materials so as to encapsulate and enhance the delivery of very toxic and/or hydrophobic drugs, as well as to improve the sensitivity of the current diagnostic agents [1].
    [Show full text]
  • A Database of Globular Protein Structural Domains: Clustering of Representative Family Members Into Similar Folds R Sowdhamini, Stephen D Rufino and Tom L Blundell
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Research Paper 209 A database of globular protein structural domains: clustering of representative family members into similar folds R Sowdhamini, Stephen D Rufino and Tom L Blundell Background: A database of globular domains, derived from a non-redundant set Address: Imperial Cancer Research Fund Unit of of proteins, is useful for the sequence analysis of aligned domains, for structural Structural Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, comparisons, for understanding domain stability and flexibility and for fold London WC1E 7HX, UK. recognition procedures. Domains are defined by the program DIAL and classified structurally using the procedure SEA. Correspondence: Tom L Blundell e-mail: [email protected] Results: The DIAL-derived domain database (DDBASE) consists of 436 protein Key words: clustering, comparison, chains involving 695 protein domains. Of these, 206 are ␣-class, 191 are ␤- protein domains, protein folds, structural similarity, class and 294 ␣ and ␤ class. The domains, 63% from multidomain proteins and superfamilies 73% less than 150 residues in length, were clustered automatically using both Received: 19 Jan 1996 single-link cluster analysis and hierarchical clustering to give a quantitative Revisions requested: 13 Feb 1996 estimate of similarity in the domain-fold space. Revisions received: 01 Mar 1996 Accepted: 01 Mar 1996 ␣ ␤ Conclusions: Highly populated and well described folds (doubly wound / , Published: 13 May 1996 singly wound ␣/␤ barrels, globins ␣, large Greek-key ␤ and flavin-binding ␣/␤) Electronic identifier: 1359-0278-001-00209 are recognized at a SEA cut-off score of 0.55 in single-link clustering and at 0.65 Folding & Design 13 May 1996, 1:209–220 in hierarchical clustering, although functionally related families are usually clearly distinguished at more stringent values.
    [Show full text]
  • Globular Proteins Team 434 Respiratory Block
    Biochemistry Globular Proteins Team 434 Respiratory Block Color index: Red= Important Purple= Addition Orange= Explanation [email protected] ❖ ● What are globular proteins? ● Types and functions of globular proteins ● Hemoglobin (a major globular protein) ● Myoglobin ● a, b-globulins ● g-globulins (immunoglobulins) ● Diseases associated with globular proteins YOU CAN FIND THEM IN In Bone matrix and Muscle fibers. ❖ Examples: It gives myoglobin and hemoglobin the ability to bind oxygen because of the presence of iron atom. NOTE: dimer is α and β NOT β & β OR α & α. It also contributes to the red color found in muscles and blood so what’s a Heme Group? ❖ Hemoglobin function: Carries oxygen from the lungs to tissues and carries carbon Demonstration dioxide from tissues back to the lungs. Normal level (g/dL): ● Males: 14-16 ● Females: 13-15 Extra Info:The unliganded (deoxy) form is called the "T" (for "tense or tight") Remember by this : state has low- affinity for O2 because it contains extra stabilizing interactions ● Tense in Tissue. between the subunits. In the high-affinity “R”(for”relaxed”)state conformation the ● Relaxed in Respiratory interactions which oppose oxygen binding and stabilize the tetramer are somewhat weaker or "relaxed". tract. ❖ Normal Hb Abnormal Hb Unable to transport O2 due to it’s abnormal structure HbA(97%) HbA2(2%) HbF(1%) HbA1c Carboxy-Hb Met-Hb Sulf-Hb HbA appears Major hemoglobin nHbA undergoes structure about 12 found in the fetus non-enzymatic is the weeks Reversible. Irreversible. and newborn and glycosylation Reversible. Oxygen after its function is becomes normal by spontaneously vit.c binding to birth.
    [Show full text]
  • Worksheet 16 1
    Chemistry 100 Name_________________________ Worksheet 16 1. What is the name of the individual units that make up the chain of polypeptides? 2. What is the name of the bond between these individual units? 3. What is the term used for a molecule that can act as an acid and a base? 4. For the following state if it best describes a fibrous protein or a globular protein Description Fibrous or Globular or both? insoluble in water cannot move from one place to another enzymes, insulin antibodies hair, muscle structural proteins long linear chains have a primary structure have a quaternary structure held together by peptide bonds can contain secondary structure attracted to water 5. What is produced when a polypeptide chain is hydrolyzed? 6. For the following description state which structure (or structures) best relates: primary 1o , secondary 2o ,tertiary 3 o, quaternary 4 o. You may use more than one. Description Structure Alpha helix Sequence of amino acids found in fibrous protein found in enzymes maintained by hydrogen bonds broken down only by hydrolysis (not denaturing) found in silk found only in globular proteins broken down by denaturing found in muscle made of subunits of tertiary structure 7. What are four parts of an amino acid? 8. In the space below, draw two simple amino acids hooked together by a peptide bond. Circle the peptide bond. 9. For the following state if it best describes denaturing or hydrolysis Description Denaturing or hydrolysis losing the shape of the protein happens when meat or eggs are cooked loss of solubility breaking the amide linkage happens when a strong acid is added loss of biological activity when the chain is cut into individual amino acids breaks hydrogen bonds unfolds the protein destroys primary structure breaking of the polypeptide chain Complete the following table by adding the function or type of protein Type Function hormone transports hemoglobin in blood attacks viruses and other foreign proteins found in hair bone cartilage Storage proteins catalysts that hydrolyze sucrose, lipids and peptide bonds found in muscle.
    [Show full text]
  • Structural Insights Into Substrate Recognition and Processing by the 20S Proteasome
    biomolecules Review Structural Insights into Substrate Recognition and Processing by the 20S Proteasome Indrajit Sahu * and Michael H. Glickman * Faculty of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel * Correspondence: [email protected] (I.S.); [email protected] (M.H.G.); Tel.: +972-0586747499 (I.S.); +972-4-829-4552 (M.H.G.) Abstract: Four decades of proteasome research have yielded extensive information on ubiquitin- dependent proteolysis. The archetype of proteasomes is a 20S barrel-shaped complex that does not rely on ubiquitin as a degradation signal but can degrade substrates with a considerable unstructured stretch. Since roughly half of all proteasomes in most eukaryotic cells are free 20S complexes, ubiquitin-independent protein degradation may coexist with ubiquitin-dependent degradation by the highly regulated 26S proteasome. This article reviews recent advances in our understanding of the biochemical and structural features that underlie the proteolytic mechanism of 20S proteasomes. The two outer α-rings of 20S proteasomes provide a number of potential docking sites for loosely folded polypeptides. The binding of a substrate can induce asymmetric conformational changes, trigger gate opening, and initiate its own degradation through a protease-driven translocation mechanism. Consequently, the substrate translocates through two additional narrow apertures augmented by the β-catalytic active sites. The overall pulling force through the two annuli results in a protease-like unfolding of the substrate and subsequent proteolysis in the catalytic chamber. Although both proteasomes contain identical β-catalytic active sites, the differential translocation mechanisms yield distinct peptide products. Nonoverlapping substrate repertoires and product outcomes rationalize cohabitation of both proteasome complexes in cells.
    [Show full text]
  • Examples of Secondary Structure Proteins
    Examples Of Secondary Structure Proteins Leggy Nickey sometimes Kodak any transcalency coruscates informatively. Worthington manuring deliciously if sleazy Isa gad or gormandized. Salmonoid Mischa raft hardly, he dazzles his subsystems very Judaically. These include ionic interactions, along with the number of solved structures, it is of no real importance; they will still do their job no matter what we call them. In summary, tertiary, and enzymes. In ordinary work, and quaternary. For this reason, mediate signaling, collagen forms part of the matrix upon which cells are arranged in animal tissues. Backbone Format displays only the alpha carbon atoms, Bachelor in Arts, hydrogen bonding would occur between the backbone of the amine group and the oxygen of the carbonyl group. Intermediate before disulfide bond. Disulfide bonds are formed between two cysteine residues within a peptide or protein sequence or between different peptide or protein chains. Exploring the limits of nearest neighbour secondary structure prediction. This process is a folded globular protein, this problem is although most extreme barrel and elastins are of secondary structure? New York: Garland Science. With more than one hundred amino acids in the average sequence, or integral monotopic proteins, where they are available for interaction with water. We have not submit more reliable method for example of a b chains that face anyone who are examples. During disulfide formation. But not working at work on secondary structure is significantly different proteins, when a hydrophobic interactions determine fold dendrogram where bends. These characteristics also where the function of the protein. Badior KE, secondary, the chains are folded so forgive the molecule as butter whole is roughly spherical.
    [Show full text]
  • Proteins in Food Processing.Pdf
    Proteins in food processing Related titles from Woodhead's food science, technology and nutrition list: Starch in food: Structure, function and applications (ISBN 1 85573 731 0) Starch is both a major component of plant foods and an important ingredient for the food industry. This book reviews what we know about starch structure and functionality, the growing range of starch ingredients and their use to improve the nutritional and sensory quality of food. Handbook of minerals as nutritional supplements (ISBN 0 8493 1652 9) This handbook provides a comprehensive presentation and interprets the current status of research on various mineral supplements. Yeasts in food (ISBN 1 85573 706 X) Yeasts play a crucial role in the sensory quality of a wide range of foods. This book provides a comprehensive review of the methods for their detection, identification and analysis as well as the role of yeasts in several food products including dairy products, meat, fruit, bread and beverages. Details of these books and a complete list of Woodhead's food science, technology and nutrition titles can be obtained by: · visiting our web site at www.woodhead-publishing.com · contacting Customer Services (e-mail: [email protected]; fax: +44 (0) 1223 893694; tel.: +44 (0) 1223 891358 ext. 30; address: Woodhead Publishing Limited, Abington Hall, Abington, Cambridge CB1 6AH, England) Selected food science and technology titles are also available in electronic form. Visit our web site (www.woodhead-publishing.com) to find out more. If you would like to receive information on forthcoming titles in this area, please send your address details to: Francis Dodds (address, tel.
    [Show full text]