Related Research Articles
An alpha helix is a sequence of amino acids in a protein that are twisted into a coil.
Collagen is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue,it is the most abundant protein in mammals,making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in connective tissue such as cartilage,bones,tendons,ligaments,and skin. Vitamin C is vital for collagen synthesis,and Vitamin E improves the production of collagen.
G protein-coupled receptors (GPCRs),also known as seven-(pass)-transmembrane domain receptors,7TM receptors,heptahelical receptors,serpentine receptors,and G protein-linked receptors (GPLR),form a large group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. They are coupled with G proteins. They pass through the cell membrane seven times in the form of six loops of amino acid residues,which is why they are sometimes referred to as seven-transmembrane receptors. Ligands can bind either to the extracellular N-terminus and loops or to the binding site within transmembrane helices. They are all activated by agonists,although a spontaneous auto-activation of an empty receptor has also been observed.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle,different intracellular membranes,the plasma membrane,or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell;errors or dysfunction in sorting have been linked to multiple diseases.
Membrane proteins are common proteins that are part of,or interact with,biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane. Peripheral membrane proteins are transiently associated with the cell membrane.
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction,although some of them (beta-barrels) can be also extracted using denaturing agents.
Peripheral membrane proteins,or extrinsic membrane proteins,are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins,or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors,for example,may be defined as peripheral membrane proteins. In contrast to integral membrane proteins,peripheral membrane proteins tend to collect in the water-soluble component,or fraction,of all the proteins extracted during a protein purification procedure. Proteins with GPI anchors are an exception to this rule and can have purification properties similar to those of integral membrane proteins.
A coiled coil is a structural motif in proteins in which 2–7 alpha-helices are coiled together like the strands of a rope. They have been found in roughly 5-10% of proteins and have a variety of functions. They are one of the most widespread motifs found in protein-protein interactions. To aid protein study,several tools have been developed to predict coiled-coils in protein structures. Many coiled coil-type proteins are involved in important biological functions,such as the regulation of gene expression —e.g.,transcription factors. Notable examples are the oncoproteins c-Fos and c-Jun,as well as the muscle protein tropomyosin.
Gramicidin,also called gramicidin D,is a mix of ionophoric antibiotics,gramicidin A,B and C,which make up about 80%,5%,and 15% of the mix,respectively. Each has 2 isoforms,so the mix has 6 different types of gramicidin molecules. They can be extracted from Brevibacillus brevis soil bacteria. Gramicidins are linear peptides with 15 amino acids. This is in contrast to unrelated gramicidin S,which is a cyclic peptide.
In chemistry,a cavitand is a container-shaped molecule. The cavity of the cavitand allows it to engage in host–guest chemistry with guest molecules of a complementary shape and size. The original definition proposed by Cram includes many classes of molecules:cyclodextrins,calixarenes,pillararenes and cucurbiturils. However,modern usage in the field of supramolecular chemistry specifically refers to cavitands formed on a resorcinarene scaffold by bridging adjacent phenolic units. The simplest bridging unit is methylene,although dimethylene,trimethylene,benzal,xylyl,pyridyl,2,3-disubstituted-quinoxaline,o-dinitrobenzyl,dialkylsilylene,and phosphonates are known. Cavitands that have an extended aromatic bridging unit,or an extended cavity containing 3 rows of aromatic rings are referred to as deep-cavity cavitands and have broad applications in host-guest chemistry. These types of cavitands were extensively investigated by Rebek,and Gibb,among others.
Bissulfosuccinimidyl suberate (BS3) is a crosslinker used in biological research. It is a water-soluble version of disuccinimidyl suberate.
HLA-G histocompatibility antigen,class I,G,also known as human leukocyte antigen G (HLA-G),is a protein that in humans is encoded by the HLA-G gene.
Andreas Mershin is a physicist at the Center for Bits and Atoms in the Massachusetts Institute of Technology.
A nanodisc is a synthetic model membrane system which assists in the study of membrane proteins. Nanodiscs are discoidal proteins in which a lipid bilayer is surrounded by molecules that are amphipathic molecules including proteins,peptides,and synthetic polymers. It is composed of a lipid bilayer of phospholipids with the hydrophobic edge screened by two amphipathic proteins. These proteins are called membrane scaffolding proteins (MSP) and align in double belt formation. Nanodiscs are structurally very similar to discoidal high-density lipoproteins (HDL) and the MSPs are modified versions of apolipoprotein A1 (apoA1),the main constituent in HDL. Nanodiscs are useful in the study of membrane proteins because they can solubilise and stabilise membrane proteins and represent a more native environment than liposomes,detergent micelles,bicelles and amphipols.
Self-assembling peptides are a category of peptides which undergo spontaneous assembling into ordered nanostructures. Originally described in 1993,these designer peptides have attracted interest in the field of nanotechnology for their potential for application in areas such as biomedical nanotechnology,tissue cell culturing,molecular electronics,and more.
Peptide amphiphiles (PAs) are peptide-based molecules that self-assemble into supramolecular nanostructures including;spherical micelles,twisted ribbons,and high-aspect-ratio nanofibers. A peptide amphiphile typically comprises a hydrophilic peptide sequence attached to a lipid tail,i.e. a hydrophobic alkyl chain with 10 to 16 carbons. Therefore,they can be considered a type of lipopeptide. A special type of PA,is constituted by alternating charged and neutral residues,in a repeated pattern,such as RADA16-I. The PAs were developed in the 1990s and the early 2000s and could be used in various medical areas including:nanocarriers,nanodrugs,and imaging agents. However,perhaps their main potential is in regenerative medicine to culture and deliver cells and growth factors.
In molecular biology,protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple,independent protein superfamilies.
The peridinin-chlorophyll-protein complex is a soluble molecular complex consisting of the peridinin-chlorophyll a-protein bound to peridinin,chlorophyll,and lipids. The peridinin molecules absorb light in the blue-green wavelengths and transfer energy to the chlorophyll molecules with extremely high efficiency. PCP complexes are found in many photosynthetic dinoflagellates,in which they may be the primary light-harvesting complexes.
The SpyTag/SpyCatcher system is a technology for irreversible conjugation of recombinant proteins. The peptide SpyTag spontaneously reacts with the protein SpyCatcher to form an intermolecular isopeptide bond between the pair. DNA sequence encoding either SpyTag or SpyCatcher can be recombinantly introduced into the DNA sequence encoding a protein of interest,forming a fusion protein. These fusion proteins can be covalently linked when mixed in a reaction through the SpyTag/SpyCatcher system.
The QTY Code is a design method to transform membrane proteins that are intrinsically insoluble in water into variants with water solubility,while retaining their structure and function.
References
- ↑ "Shuguang Zhang, MIT Media Lab, People". MIT Media Lab.
- ↑ "Shuguang Zhang". scholar.google.com.
- ↑ "ORCiD Shuguang Zhang".
- ↑ Baas, Jeroen (2020). "Bibliometrics". Mendeley Data. Vol. 2. Mendeley. doi:10.17632/btchxktzyw.2.
- ↑ "Molecular Frontiers Board of Directors".
- ↑ "Molecular Frontiers Symposia".
- ↑ "Molecular Frontiers Inquiry Prize".
- ↑ Zhang, Shuguang (October 20, 2017). "Discovery and design of self-assembling peptides". Interface Focus. 7 (6): 20170028. doi:10.1098/rsfs.2017.0028. PMC 5665798 . PMID 29147558.
- ↑ Zhang, Shuguang (October 11, 1992). "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae". The EMBO Journal. 11 (10): 3787–3796. doi:10.1002/j.1460-2075.1992.tb05464.x. PMC 556839 . PMID 1396572.
- ↑ "John Simon Guggenheim Foundation - Shuguang Zhang".
- ↑ Levin, Aviad (September 15, 2020). "Biomimetic peptide self-assembly for functional materials". Nature Reviews Chemistry. 4 (11): 615–634. doi:10.1038/s41570-020-0215-y. S2CID 221718855.
- ↑ Gelain, Fabrizio (February 17, 2021). "Self-assembling peptide scaffolds in the clinic". npj Regenerative Medicine. 6 (1): 9. doi:10.1038/s41536-020-00116-w. PMC 7889856 . PMID 33597509.
- ↑ Yang, Jia (2021). "Self-Assembled Peptide Drug Delivery Systems". ACS Appl. Bio. Mater. 4 (1): 24–46. doi:10.1021/acsabm.0c00707. PMID 35014275. S2CID 225639201.
- ↑ "About - 3-D Matrix".
- ↑ Gelain, Fabrizio; Luo, Zhongli; Rioult, Marika; Zhang, Shuguang (17 February 2021). "Self-assembling peptide scaffolds in the clinic". npj Regenerative Medicine. 6 (1): 9. doi: 10.1038/s41536-020-00116-w . PMC 7889856 . PMID 33597509. S2CID 231948060.
- 1 2 3 Zhang, Shuguang (September 11, 2018). "QTY code enables design of detergent-free chemokine receptors that retain ligand-binding activities". Proc. Natl. Acad. Sci. USA. 115 (37): E8652–E8659. Bibcode:2018PNAS..115E8652Z. doi: 10.1073/pnas.1811031115 . PMC 6140526 . PMID 30154163.
- ↑ Qing, Rui (December 17, 2019). "QTY code designed thermostable and water-soluble chimeric chemokine receptors with tunable ligand affinity". Proc. Natl. Acad. Sci. USA. 116 (51): 25668–25676. Bibcode:2019PNAS..11625668Q. doi: 10.1073/pnas.1909026116 . PMC 6926000 . PMID 31776256.
- 1 2 Arnaud, Celia (August 29, 2018). "Following a code for swapping amino acids makes membrane proteins water soluble". Chemical & Engineering News. 96.
- ↑ Trafton, Anne (August 28, 2018). "Scientists alter membrane proteins to make them easier to study". Phys.org.
- ↑ Fagerberg, Linn; Jonasson, Kalle; Von Heijne, Gunnar; Uhlén, Mathias; Berglund, Lisa (19 March 2010). "Prediction of the human membrane proteome". Proteomics. 10 (6): 1141–1149. doi:10.1002/pmic.200900258. PMID 20175080. S2CID 5082887.
- ↑ Wallin, Erik; Von Heijne, Gunnar (31 December 2008). "Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms". Protein Science. 7 (4): 1029–1038. doi:10.1002/pro.5560070420. PMC 2143985 . PMID 9568909.
- ↑ "John Simon Guggenheim Foundation - Shuguang Zhang".
- ↑ "Cambridge vs. Cambridge: a personal comparison - News Article on Nature Network Boston" (PDF).
- ↑ "Shuguang Zhang - Wilheim Exner Medaillen Stiftung".
- ↑ "ÖAW Mitglieder Detail".
- ↑ "Shuguang Zhang, Ph.D. COF-1267 - AIMBE".
- ↑ "National Academy of Inventors".
- ↑ "Shuguang Zhang receives Emil Thomas Kaiser Award – MIT Media Lab".
- ↑ "Members - European Academy of Sciences and Arts".
- ↑ "flyer-20th-colloquium.pdf" (PDF).
