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Protein
Technologies glossary & taxonomy
Evolving Terminology for Emerging Technologies
Comments? Questions?
Revisions? Mary Chitty MSLS
mchitty@healthtech.com
Last revised
September 12, 2019
Drug
discovery & development term index Informatics
term index Technologies term
index Biology term index
Chemistry term index
Related glossaries include
Bioprocessing & manufacturingg
Labels
Signaling & Detection Mass
Spectrometry NMR & x-ray
crystallography Proteomics
PEGS:
the essential protein engineering summit
May 4-8, 2020 • Boston, MA Program | Conference
programs include protein and antibody engineering, cancer immunotherapy,
oncology, and emerging therapeutics.
PEGS Europe
2018 Nov 12-16 Lisbon Portugal
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covers a wide spectrum of applied protein sciences with emphasis on upstream R&D
engineering to downstream biologics production.

2D gel electrophoresis:
A key technology for proteomics.
Chromatography
& electrophoresis glossary
antibody
display: de Kruif
J,, Boel E, Logtenberg T. Selection
and application of human single chain Fv antibody fragments from a
semi-synthetic phage antibody display library with designed CDR3 regions.
J Mol Biol. 1995 Apr 21;248 (1): 97-105, April 1995 .
aptamer: Aptamers are short
nucleic acid sequences capable of specific, high-affinity molecular binding.
They are isolated via SELEX (Systematic Evolution of Ligands by Exponential
Enrichment), an evolutionary process that involves iterative rounds of selection
and amplification before sequencing and aptamer characterization. As aptamers
are genetic in nature, bioinformatic approaches have been used to improve both
aptamers and their selection. Kinghorn AB, Fraser LA, Liang S, Shiu SC-C, Tanner
JA. Aptamer Bioinformatics. International Journal of Molecular Sciences.
2017;18(12):2516. doi:10.3390/ijms18122516.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751119/
A synthetic, specially- designed oligonucleotide with
the ability to recognize and bind a protein ligand molecule or molecules
with high affinity and specificity. Narrower terms:
photoaptamers, Functional
genomics Protein technologies
peptide aptamer; Genomic technologies
SELEX,
spielgemers
bacteriophage:
Many phage have proved useful in the study of
molecular biology and as vectors for the transfer of genetic information
between cells … lambda bacteriophage can also undergo a lytic cycle or
can enter a lysogenic cycle, in which the page DNA is incorporated into
that of the host, awaiting a signal that initiates events leading to replication
of the virus and lysis of the host cell. Glick
The workhorse of phage display is the M13 bacteriophage virus. Related terms: phage,
phage display bacteriophage, biopanning, phage; Labels, signaling & detection
Proteomics directed protein evolution
bait: The basic format of the yeast-two hybrid system involves the creation of two hybrid
molecules, one in which the "bait" protein is fused with
a transcription factor, and one in which the "prey" protein
is fused with a related transcription factor. If the bait and prey proteins
indeed interact then the two factors fused to these two proteins are also
brought into proximity with each other. As a result a specific signal is
produced, indicating an interaction has taken place.
carbohydrate chips:
University scientists have described the first
chip- based chemical strategy for rapidly screening carbohydrates for
biologically useful activity. [Chemical method makes further investigation of
carbohydrates possible, Univ. of Chicago Chronicle, 21 (3) April 11, 2002]
http://chronicle.uchicago.edu/020411/biochip.shtml
carbohydrate
microarrays: Stu Borman, Chemical and
Engineering News, Dec. 16, 2002 lists as highlights of 2002 http://pubs.acs.org/cen/coverstory/8050/8050chemhighlights5.html
with references to the literature on polysaccharide and glycoconjugate
microarrays, monosaccharide chips, natural and synthetic oligosaccharide arrays,
and synthetic oligosaccharides in microtiter plate format.
cDNA phage display:
Display
cloning: functional identification of natural product receptors using cDNA-phage
display. Sche PP, McKenzie KM, White JD, Austin DJ. Chem Biol. 1999
Oct;6(10):707- 716
co-immunoprecipitation
Used to determine protein- protein
interactions. An antibody is used to precipitate a protein along
with bound proteins. John Yates, “Mass spectrometry and the Age of the
Proteome” Journal Mass Spectrometry 33: 16, 1998
combinatorial biology:
the creation of a large number of compounds
(usually proteins or peptides) through technologies such as phage
display. Similar to combinatorial
chemistry, compounds are produced by biosynthesis rather
than organic chemistry.
This process was developed independently by Richard
A. Houghten and H. Mario Geysen in the 1980s. Combinatorial biology allows
the generation and selection of the large number of ligands for high-throughput
screening.[1][2]
Combinatorial biology techniques generally begin with large numbers of peptides,
which are generated and screened by physically linking a gene encoding a protein
and a copy of said protein. This could involve the protein being fused to the M13 minor
coat protein pIII, with the gene encoding this protein being held within the
phage particle. Large libraries of phages with different proteins on their
surfaces can then be screened through automated selection and amplification for
a protein that binds tightly to a particular target.[3]
Wikipedia accessed 2018 Nov 8
https://en.wikipedia.org/wiki/Combinatorial_biology
Related term: phage display
co-precipitation:
Method to identify interacting proteins by
using antibodies to bind to the protein if immunoprecipitated under non-
denaturing
using conditions … (allow any other proteins bound to the protein known
to be involved in a process) to precipitate rather than be washed away.
depletion: Method of sample preparation which removes high
abundance proteins (not of interest) from the sample. Related
term: low- abundance proteins.
directed evolution:
Directed Evolution-Based Drug
Discovery DNA Encoded Libraries and Other Diversity Oriented Platforms
APRIL 9-10, 2019 San Diego CA Directed evolution approaches for drug
discovery use genetic strategies (DNA-encoded, RNA-encoded or phage-based)
to create very large but specific libraries of molecules whose
amplification is driven by the target of interest. The theory was
established decades ago but recently applications in early stage drug
discovery have become more widespread. A few drug candidates arising from
directed evolution campaigns are now in clinical trials. A bottleneck
however of these diversity-oriented strategies is figuring out which hits
to focus on from the many hits that are produced by these approaches.
https://www.drugdiscoverychemistry.com/Directed-Evolution
a method used in protein
engineering that
mimics the process of natural
selection to
evolve proteins or nucleic
acids toward
a user-defined goal.[1] It
consists of subjecting a gene to
iterative rounds of mutagenesis (creating a library of variants),
selection (expressing the variants and isolating members with the desired
function), and amplification (generating a template for the next round).
It can be performed in vivo (in living cells), or in vitro (free
in solution or microdroplet). Directed evolution is used both for protein
engineering as
an alternative to rationally designing modified proteins, as well as
studies of fundamental evolutionary
principles in
a controlled, laboratory environment. Wikipedia accessed 2018 Sept 3
https://en.wikipedia.org/wiki/Directed_evolution
Directed evolution is an iterative process scientists use to design
biological molecules like enzymes. It requires
inducing some randomness in the target enzyme within an organism like
bacteria. The resulting mutated bacteria are screened to see which ones do
the intended job the best. The winners are then cultured, and from their
offspring, the best are selected, and then cultured, and so on.
https://www.vox.com/science-and-health/2018/10/3/17931612/nobel-prize-2018-chemistry-directed-evolution-enzymes-antibodies
directed protein evolution:
Systematic approaches to directed
evolution of proteins have been documented since the 1970s. The ability to
recruit new protein functions arises from the considerable substrate
ambiguity of many proteins. The substrate ambiguity of a protein can be
interpreted as the evolutionary potential that allows a protein to acquire
new specificities through mutation or to regain function via mutations
that differ from the original protein sequence. All organisms have
evolutionarily exploited this substrate ambiguity. When exploited in a
laboratory under controlled mutagenesis and selection, it enables a
protein to “evolve” in desired directions. One of the most effective
strategies in directed protein evolution is to gradually accumulate
mutations, either sequentially or by recombination, while applying
selective pressure. This is typically achieved by the generation of
libraries of mutants followed by efficient screening of these libraries
for targeted functions and subsequent repetition of the process using
improved mutants from the previous screening. Here we review some of the
successful strategies in creating protein diversity Yuan L, Kurek I,
English J, Keenan R. Laboratory-Directed Protein Evolution. Microbiology
and Molecular Biology Reviews. 2005;69(3):373-392.
doi:10.1128/MMBR.69.3.373-392.2005.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1197809/
Related term: phage display
display of antibodies
2019 April 8-9 Boston MA
showcases innovation in discovery, design and engineering of biologics
through molecular evolution using phage, yeast and other display
methodologies. The proliferation of novel constructs is possible through
methods to improve library design, pharmacological and biophysical
properties to create drug molecules with greater potency, modes of action,
target specificity and activity than previously achievable.
Related terms:
phage display, yeast display
DNA
shuffling: Genomic technologies
Can
be used to evolve proteins.
gene
shuffling: Genomic technologies
Can
be used to evolve proteins.
glycoarrays:
Carbohydrate arrays (glycoarrays) have recently
emerged as a high-throughput tool for
studying carbohydrate-binding proteins and carbohydrate-processing enzymes. A
number of sophisticated array platforms that allow for qualitative
and quantitative analysis of carbohydrate binding and modification on the array
surface have been developed, including analysis by fluorescence
spectroscopy, mass spectrometry and surface plasmon resonance
spectroscopy. Glycoarrays--tools for determining protein-carbohydrate
interactions and glycoenzyme specificity.
Laurent N1, Voglmeir
J, Flitsch
SL. Chem Commun
(Camb). 2008 Oct 7;(37):4400-12. doi: 10.1039/b806983m. Epub 2008 Aug 5.
https://pubs.rsc.org/en/Content/ArticleLanding/CC/2008/B806699J#!divAbstract
https://www.ncbi.nlm.nih.gov/pubmed/18802573
glycoprotein
microarrays: We employ carbohydrate and glycoprotein microarrays to
analyze glycan- dependent gp120- protein interactions. In concert with new
linking chemistries and synthetic methods, the carbohydrate arrays combine the
advantages of microarray technology with the flexibility and precision afforded
by organic synthesis. With these microarrays, we individually and competitively
determined the binding profiles of five gp120 binding proteins, established the
carbohydrate structural requirements for these interactions, and identified a
potential strategy for HIV vaccine development. EW Adams et. al., Oligosaccharide
and glycoprotein microarrays as tools in HIV glycobiology; glycan- dependent
gp120/ protein interactions, Chem Biol. 11(6): 875- 881, June 2004
Related terms:
oligosaccharide chips; Glycosciences glossary
intrabodies:
Recent advances in antibody engineering have now allowed
the genes encoding antibodies to be manipulated so that the antigen binding
domain can be expressed intracellularly. The specific and high- affinity binding
properties of antibodies, combined with their ability to be stably expressed in
precise intracellular locations inside mammalian cells, has provided a powerful
new family of molecules for gene therapy applications. These
intracellular antibodies are termed 'intrabodies'. Wayne A. Marasco, "Intrabodies:
turning the humoral immune system outside in for intracellular
immunization" Gene Therapy 4 (1): 11- 15, Jan. 1997
Isotope Coded Infinity Tag ICAT:
These tags provide the ability
to both identify and quantify a broad range of proteins in a high- throughput
mode. Using ICAT reagents, researchers can compare the expression levels of
proteins from two samples, such as from normal and diseased cells. ICAT reagents
comprise a protein reactive group, an affinity tag (biotin), and an
isotopically labeled linker. Related term:
protein profiling
molecular evolution
protein: Evolution of proteins is studied by comparing the
sequences and structures of proteins from many organisms representing
distinct evolutionary clades. If the sequences/structures of two proteins
are similar indicating that the proteins diverged from a common origin,
these proteins are called as homologous proteins. More specifically,
homologous proteins that exist in two distinct species are called as
orthologs. Whereas, homologous proteins encoded by the genome of a single
species are called paralogs. Wikipedia accessed 2018 Nov 10
https://en.wikipedia.org/wiki/Molecular_evolution#Protein_evolution
molecular protein
evolution directed: Systematic approaches to directed evolution
of proteins have been documented since the 1970s. The ability to recruit
new protein functions arises from the considerable substrate ambiguity of
many proteins. The substrate ambiguity of a protein can be interpreted as
the evolutionary potential that allows a protein to acquire new
specificities through mutation or to regain function via mutations that
differ from the original protein sequence. All organisms have
evolutionarily exploited this substrate ambiguity. When exploited in a
laboratory under controlled mutagenesis and selection, it enables a
protein to “evolve” in desired directions. One of the most effective
strategies in directed protein evolution is to gradually accumulate
mutations, either sequentially or by recombination, while applying
selective pressure. This is typically achieved by the generation of
libraries of mutants followed by efficient screening of these libraries
for targeted functions and subsequent repetition of the process using
improved mutants from the previous screening. Here we review some of the
successful strategies in creating protein diversity Yuan L, Kurek I,
English J, Keenan R. Laboratory-Directed Protein Evolution. Microbiology
and Molecular Biology Reviews. 2005;69(3):373-392.
doi:10.1128/MMBR.69.3.373-392.2005.https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1197809/
molecular motors:
Protein based machines that are involved in
or cause movement such as the rotary devices (flagellar motor and the F1
ATPase) or the devices whose movement is directed along cytoskeletal filaments
(myosin, kinesin and dynein motor families). MeSH, 1999
Wikipedia http://en.wikipedia.org/wiki/Molecular_motors
oligosaccharide
microarrays:
Studies on glycans are
indispensable to define complex life systems and cell communities because all
living organisms consist of diverse cells, which are covered with an abundance
of heterogeneous carbohydrates. Although studies on glycans are extremely
difficult because of the lack of basic technologies common to DNAs and proteins,
a few new aspects of glycotechnologies have now become realized in the form of
'bio- chips', which include 'oligosaccharide arrays' or 'glyco- chips'.
Recently, Fukui et al. developed oligosaccharide microarrays for glycomic analysis
of extensive carbohydrate- binding proteins. How and why such glyco- engineering
projects have been made in the contexts of both pure and applied sciences is
described. J. Hirabayashi, Oligosaccharide microarrays for
glycomics, Trends in
Biotechnology 21 (4): 141-143, Apr. 2003
Related terms:
glycochip, glycoprotein arrays
peptide
aptamers:
Engineered protein molecules selected from
combinatorial libraries, [used] to dissect the function of specific genes and
alleles, and to trace genetic pathways. Roger Brent "Peptide
aptamers" Molecular Sciences Institute, 1999 Broader term: aptamers
peptide arrays: Steve Fodor and colleagues at Affymax published
several articles on these in the early 1990s.
Related terms
protein arrays,
protein chips, protein microarrays
Peptide Mass Fingerprinting PMF:
A means of protein identification,
using mass spectrometry
peptide sequencing:
How is this different from protein sequencing
(except that peptides are shorter than proteins)?
phage:
A virus for which the natural host is a bacterial cell.
DOE
Used as a vector for cloning segments of DNA.
Schlindwein Related terms: bacteriophage, phage display.
phage display:
Antibody
Display
May 4-5, 2020 • Boston, MA Program | cornerstone
conference of the PEGS Summit and convenes leaders in the field year after
year. This year’s meeting showcases innovation in discovery, design and
engineering of biologics through molecular evolution using phage, yeast and
other display methodologies. The proliferation of novel constructs is possible
through methods to improve library design, pharmacological and biophysical
properties to create drug molecules with greater potency, modes of action,
target specificity and activity than previously achievable.
Use of genetically engineered phage to present
peptides as segments of their native surface proteins. Peptide libraries may be produced by populations
of phage with different gene sequences. IUPAC Combinatorial Chemistry Broader
term: display technologies Related terms:
bacteriophage, biopanning, phage; Labels, signaling & detection; Proteomics directed protein evolution
photoaptamers:
Aptamers that
incorporate a brominated deoxyuridine (BrdU) in place of the thymidine (T)
normally found in DNA. A photoaptamer recognizes both the complex shape and
charge distribution of its protein target and the presence of specific amino
acid residues at specific sites. Related term: spiegelmer; Broader term: aptamers
prefractionation:
Sample preparation
method, capable of being automated.
protein arrays:
Protein arrays are poised to become a central proteomics
technology allowing for the global observation of biochemical activities on an
unprecedented scale. Hundreds or thousands of proteins can be simultaneously
screened for protein-protein, protein-nucleic acid, and small molecule
interactions. The value of multiplexed protein measurement is being established
in applications including: comprehensive proteomic surveys, studies of protein
networks and pathways, validation of genomic discoveries, and clinical biomarker
development. This technology holds great potential for basic molecular biology
research, serum profiling, protein abundance determination, disease biomarker
identification, immune and toxicological response profiling, and pharmaceutical
target screening.
Related terms: antibody arrays, protein chips, protein microarrays
Narrower
terms: high- density protein arrays, protein-
protein
interaction chips, proteome chip
protein capture
reagents:
The Common Fund’s Protein Capture Reagents
program is developing new resources and tools to understand the critical role
the multitude of cellular proteins play in normal development and health as well
as in disease. These resources will support a wide-range of research and
clinical applications that will enable the isolation and tracking of proteins of
interest and permit their use as diagnostic biomarkers of disease onset and
progression. NIH Common Fund http://commonfund.nih.gov/proteincapture/
protein chips:
The protein chip is not going to
replace certain discovery methods (such as 2D gel
electrophoresis), which are
very good at identifying novel proteins in a complex mixture. Perhaps the
greatest limitation of methods based on electrophoresis is that they are
relatively expensive to perform in terms of the cost per data point, and can be
quite laborious. The trend, however, may continue toward reduced costs and ease
of use. Another limitation of conventional proteomic methods is that they may
not be versatile enough to rapidly gather biological information - changes in
protein expression, protein- protein
interactions, response to various
conditions.
Ciphergen trademarked ProteinChip™
which is now owned by BioRad. Some chips can operate with both nucleic acids and proteins. Analogous
to DNA chips, these are used for studying
protein expression
or protein- protein interactions. Related terms: antibody
arrays, carbohydrate chips, carbohydrate arrays, protein arrays, protein microarrays; Narrower
terms: high- density protein microarrays, protein-protein
interaction chips, proteome chip
protein engineering:
A technique used to produce proteins with altered or novel amino acid sequences. The methods used are: 1.
Transcription and translation systems from synthesized lengths of DNA or RNA with novel sequences. 2. Chemical modification of
'normal' proteins. 3. Solid- state polypeptide
synthesis to form proteins. IUPAC Compendium
Procedures by which protein structure and
function are changed or created in vitro by altering existing or synthesizing
new structural genes that direct the synthesis of proteins with sought-after
properties. Such procedures may include the design of MOLECULAR
MODELS of proteins using COMPUTER
GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS,
SITE-SPECIFIC) of existing genes; and DIRECTED
MOLECULAR EVOLUTION techniques to create new genes. MeSH 2003
the process of
developing useful or valuable proteins. It is a young discipline, with
much research taking place into the understanding of protein
folding and recognition for protein
design principles. It is also a product and services market, with an
estimated value of $168 billion by 2017.[1]
...There
are two general strategies for protein engineering: rational
protein design and directed evolution. These methods are not
mutually exclusive; researchers will often apply both. In the future, more
detailed knowledge of protein structure and function,
and advances in high-throughput
screening, may greatly expand the abilities of protein
engineering. Eventually, even unnatural amino acids may be included, via
newer methods, such as expanded genetic code, that allow encoding
novel amino acids in genetic code. Wikipedia accessed 2018 Sept 5
Wikipedia
http://en.wikipedia.org/wiki/Protein_engineering
PEGS:
the essential protein engineering summit
May 4-5, 2020 •
Boston, MA Program |
protein inhibition:
An alternative approach to [gene
expression] downregulation, but in this case, the protein, not the gene, is the
target. As with downregulation of gene expression, protein inhibition is a
powerful target validation tool. The major approach to protein inhibition
is based on phage libraries, which are used to select antibodies against
targets of interest.
protein knockouts:
deGradFP (degrade Green Fluorescent Protein), an
easy-to-implement protein knockout method applicable in any eukaryotic
genetic system. Depleting a protein in order to study its function in a
living organism is usually achieved at the gene level (genetic mutations)
or at the RNA level (RNA interference and morpholinos). However, any
system that acts upstream of the proteic level depends on the turnover
rate of the existing target protein, which can be extremely slow. In
contrast, deGradFP is a fast method that directly depletes GFP fusion
proteins. In particular, deGradFP is able to counteract maternal effects
in embryos and causes early and fast onset loss-of-function phenotypes of
maternally contributed proteins.
Protein Knockouts in Living Eukaryotes Using deGradFP and Green
Fluorescent Protein Fusion Targets
Current protocols in protein science /
editorial board, John E. Coligan ... [et al.] 73(73):30.2.1-30.2.13 · September
2013 DOI: 10.1002/0471140864.ps3002s7
https://www.ncbi.nlm.nih.gov/pubmed/24510595
protein localization:
There is an ever- increasing number of genes
that have been sequenced but are of completely unknown function. The ability to
determine the location of such gene products within the cell, either by the use
of antibodies or by the production of chimeras with green fluorescent
protein, is a vital step towards understanding what they do. This is one
major reason why fluorescence microscopy is enjoying a revival.
Protein
Localization by Fluorescence Microscopy: A Practical Approach Edited by VICTORIA
J. ALLAN, Oxford University Press, 2000
Narrower terms: subcellular localization,
tissue specific localization;
Related terms Cell biology: subcellular fractionation;
Gene definitions: gene localization; Omes
& omics localizome
protein microarrays:
These arrays can consist of proteins themselves
(e.g., for studies of protein/ protein interactions or protein/ small- molecule
binding) or of probes for capturing proteins (so that protein levels in a sample
can be gauged).
Protein
microarrays will permit researchers to scan thousands of proteins in a variety
of proteomic experiments, including differential expression, response to drugs,
protein- protein interactions and identification of disease biomarkers. So far,
they have proven to be very quantitative and, by virtue of their addressable
arrays, much easier to compare results between experiments than 2D gels.
Commercialization of protein arrays also promises rapid development toward real
applications in clinical and point- of- care diagnostics, which would be
impossible with more complex proteomic technologies that require
electrophoresis
or chromatography. One disadvantage of the microarray approach is that generally
it is a "closed" system - you can only measure proteins for which you
have a capturing agent (such as an antibody).
Related
terms: antibody microarrays, protein arrays, protein chips, protein profiling
chips; Narrower terms: electrospray-
fabricated protein microarrays, functional protein microarrays, protein-protein
interaction chips, proteome chip Wikipedia
http://en.wikipedia.org/wiki/Protein_microarray
protein purification: John
Wagner's Logic of Molecular Approaches to Biological Problems (Cornell
Univ. Graduate School of Medical Science, US ) has a section on the value
of protein purification. http://www-users.med.cornell.edu/~jawagne/proteins_%26_purification.html
proteolysis: Wikipedia http://en.wikipedia.org/wiki/Proteolysis
Research and diagnostic applications
proteolytic processing: Related terms proteolysis Broader term post-
translational modification
proteomics technologies: Major
types include protein separation, ultrafiltration, 1D and 2D gel electrophoresis,
liquid chromatography, capillary electrophoresis, mass
spectrometry, protein informatics,protein
arrays, protein quantification, protein localization, and protein-
protein interactions.
The application of proteomics technologies to clinical research and public
health in general is an immediate goal of proteomics. A distantly related
goal is the eventual application of proteomics to environmental,
agricultural and veterinary research, research areas that are far less
developed than clinical applications. Defining the Mandate of Proteomics
in the Post- Genomics Era, Board on International Scientific
Organizations, National Academy of Sciences, 2002 http://www.nap.edu/books/NI000479/html/R1.html
For a field so laden with razzmatazz methods, it is striking that the
number one need in proteomics may be new technology. There are simply not
enough assays that are sufficiently streamlined to allow the automation
necessary to perform them on a genome's worth of proteins. Those currently
available barely scratch the surface of the thousands of specialized
analyses biologists use every day on their favorite proteins. What we need
are experimental strategies that could be termed cell biological genomics,
biophysical genomics, physiological
genomics, and so on, to provide clues to function. In addition, a
protein contains so many types of information that each of its properties
needs to be assayed on a proteome- wide scale, ideally in a quantitative
manner. Stanley Fields "Proteomics in Genomeland" Science 291: 1221-1224
Feb. 16, 2001
self-assembling biomolecular materials: Examples
of self- assembly include protein folding, the formation of liposomes, and
the alignment of liquid crystals. While this type of equilibrium self-
assembly is the central focus of this report, it is important to emphasize
that much biological assembly is also driven by energy sources such as
adenosine triphosphate (ATP), which power biomotors Biomolecular
self- assembling materials, National Academy of Sciences 1996 http://www.nas.edu/bpa/reports/bmm/bmm.html#PBMM Broader
term: self-assembly
subcellular localization: A
variety of approaches—including tagging and fluorescence technologies,
cellular isolation methods, gels, and mass spectrometry—are being used in
these studies, which aim to track the location and/or movement of proteins
or protein complexes in subcellular compartments.
translation: Sequences,
DNA & beyond Another
approach to downregulating gene expression See
also Pharmaceutical
biology antisense; RNA
ribozymes.
yeast display: (or yeast surface display):
a protein
engineering technique that uses the expression of recombinant
proteins incorporated into the cell wall of yeast for
isolating and engineering antibodies.
Wikipedia accessed 2018 Oct 27
https://en.wikipedia.org/wiki/Yeast_display
Protein technologies resources
NFCR Center for Therapeutic Antibody Engineering Glossary, National
Foundation for Cancer Research, Dana Farber Cancer Institute http://research4.dfci.harvard.edu/nfcr-ctae/research/tech_glossary.php
How to look for other
unfamiliar terms
IUPAC definitions are reprinted with the permission of the International
Union of Pure and Applied Chemistry.
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