Related Research Articles
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms,including catalysing metabolic reactions,DNA replication,responding to stimuli,providing structure to cells and organisms,and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids,which is dictated by the nucleotide sequence of their genes,and which usually results in protein folding into a specific 3D structure that determines its activity.
Biophysics is an interdisciplinary science that applies approaches and methods traditionally used in physics to study biological phenomena. Biophysics covers all scales of biological organization,from molecular to organismic and populations. Biophysical research shares significant overlap with biochemistry,molecular biology,physical chemistry,physiology,nanotechnology,bioengineering,computational biology,biomechanics,developmental biology and systems biology.
Force spectroscopy is a set of techniques for the study of the interactions and the binding forces between individual molecules. These methods can be used to measure the mechanical properties of single polymer molecules or proteins,or individual chemical bonds. The name "force spectroscopy",although widely used in the scientific community,is somewhat misleading,because there is no true matter-radiation interaction.
Atomic force microscopy (AFM) or scanning force microscopy (SFM) is a very-high-resolution type of scanning probe microscopy (SPM),with demonstrated resolution on the order of fractions of a nanometer,more than 1000 times better than the optical diffraction limit.
Bacteriorhodopsin (Bop) is a protein used by Archaea,most notably by haloarchaea,a class of the Euryarchaeota. It acts as a proton pump;that is,it captures light energy and uses it to move protons across the membrane out of the cell. The resulting proton gradient is subsequently converted into chemical energy.
The plasma membranes of cells contain combinations of glycosphingolipids,cholesterol and protein receptors organised in glycolipoprotein lipid microdomains termed lipid rafts. Their existence in cellular membranes remains controversial. Indeed,Kervin and Overduin imply that lipid rafts are misconstrued protein islands,which they propose form through a proteolipid code. Nonetheless,it has been proposed that they are specialized membrane microdomains which compartmentalize cellular processes by serving as organising centers for the assembly of signaling molecules,allowing a closer interaction of protein receptors and their effectors to promote kinetically favorable interactions necessary for the signal transduction. Lipid rafts influence membrane fluidity and membrane protein trafficking,thereby regulating neurotransmission and receptor trafficking. Lipid rafts are more ordered and tightly packed than the surrounding bilayer,but float freely within the membrane bilayer. Although more common in the cell membrane,lipid rafts have also been reported in other parts of the cell,such as the Golgi apparatus and lysosomes.
Biomolecular structure is the intricate folded,three-dimensional shape that is formed by a molecule of protein,DNA,or RNA,and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels:primary,secondary,tertiary,and quaternary. The scaffold for this multiscale organization of the molecule arises at the secondary level,where the fundamental structural elements are the molecule's various hydrogen bonds. This leads to several recognizable domains of protein structure and nucleic acid structure,including such secondary-structure features as alpha helixes and beta sheets for proteins,and hairpin loops,bulges,and internal loops for nucleic acids. The terms primary,secondary,tertiary,and quaternary structure were introduced by Kaj Ulrik Linderstrøm-Lang in his 1951 Lane Medical Lectures at Stanford University.
Scanning ion-conductance microscopy (SICM) is a scanning probe microscopy technique that uses an electrode as the probe tip. SICM allows for the determination of the surface topography of micrometer and even nanometer-range structures in aqueous media conducting electrolytes. The samples can be hard or soft,are generally non-conducting,and the non-destructive nature of the measurement allows for the observation of living tissues and cells,and biological samples in general.
Molecular biophysics is a rapidly evolving interdisciplinary area of research that combines concepts in physics,chemistry,engineering,mathematics and biology. It seeks to understand biomolecular systems and explain biological function in terms of molecular structure,structural organization,and dynamic behaviour at various levels of complexity. This discipline covers topics such as the measurement of molecular forces,molecular associations,allosteric interactions,Brownian motion,and cable theory. Additional areas of study can be found on Outline of Biophysics. The discipline has required development of specialized equipment and procedures capable of imaging and manipulating minute living structures,as well as novel experimental approaches.
In chemistry and materials science,molecular self-assembly is the process by which molecules adopt a defined arrangement without guidance or management from an outside source. There are two types of self-assembly:intermolecular and intramolecular. Commonly,the term molecular self-assembly refers to the former,while the latter is more commonly called folding.
Photothermal microspectroscopy (PTMS),alternatively known as photothermal temperature fluctuation (PTTF),is derived from two parent instrumental techniques:infrared spectroscopy and atomic force microscopy (AFM). In one particular type of AFM,known as scanning thermal microscopy (SThM),the imaging probe is a sub-miniature temperature sensor,which may be a thermocouple or a resistance thermometer. This same type of detector is employed in a PTMS instrument,enabling it to provide AFM/SThM images:However,the chief additional use of PTMS is to yield infrared spectra from sample regions below a micrometer,as outlined below.
Helen Miriam Berman is a Board of Governors Professor of Chemistry and Chemical Biology at Rutgers University and a former director of the RCSB Protein Data Bank. A structural biologist,her work includes structural analysis of protein-nucleic acid complexes,and the role of water in molecular interactions. She is also the founder and director of the Nucleic Acid Database,and led the Protein Structure Initiative Structural Genomics Knowledgebase.
Single-particle tracking (SPT) is the observation of the motion of individual particles within a medium. The coordinates time series,which can be either in two dimensions (x,y) or in three dimensions (x,y,z),is referred to as a trajectory. The trajectory is typically analyzed using statistical methods to extract information about the underlying dynamics of the particle. These dynamics can reveal information about the type of transport being observed (e.g.,thermal or active),the medium where the particle is moving,and interactions with other particles. In the case of random motion,trajectory analysis can be used to measure the diffusion coefficient.
A model lipid bilayer is any bilayer assembled in vitro,as opposed to the bilayer of natural cell membranes or covering various sub-cellular structures like the nucleus. They are used to study the fundamental properties of biological membranes in a simplified and well-controlled environment,and increasingly in bottom-up synthetic biology for the construction of artificial cells. A model bilayer can be made with either synthetic or natural lipids. The simplest model systems contain only a single pure synthetic lipid. More physiologically relevant model bilayers can be made with mixtures of several synthetic or natural lipids.
NanoWorld is the global market leader for tips for scanning probe microscopy (SPM) and atomic force microscopy (AFM). The atomic force microscope (AFM) is the defining instrument for the whole field of nanoscience and nanotechnology. It enables its users in research and high-tech industry to investigate materials at the atomic scale. AFM probes are the key consumable,the “finger”that enables the scientist to scan surfaces point-by-point at the atomic scale. Consistent high quality of the scanning probes is vital for reproducible results.
NanoAndMore is a distributor for AFM cantilevers from NanoWorld,Nanosensors,BudgetSensors,MikroMasch,Opus and nanotools,calibration standards and other products for nanotechnology.
In molecular biology,the term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles,cellular organelles and membranes and ribosomes,etc. that are complex mixtures of polypeptide,polynucleotide,polysaccharide or other polymeric macromolecules. They are generally of more than one of these types,and the mixtures are defined spatially,and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things,and are composed of many hundreds or thousands of atoms held together by covalent bonds;they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic,though the MA term is more commonly applied in biology,and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions,and can be in either non-repeating structures,or in repeating linear,circular,spiral,or other patterns. The process by which MAs are formed has been termed molecular self-assembly,a term especially applied in non-biologic contexts. A wide variety of physical/biophysical,chemical/biochemical,and computational methods exist for the study of MA;given the scale of MAs,efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.
Paul K. Hansma is an American physicist at the University of California,Santa Barbara.
Mei Hong is a Chinese-American biophysical chemist and professor of chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins,plant cell walls,and amyloid proteins. She has received a number of recognitions for her work,including the American Chemical Society Nakanishi Prize in 2021,Günther Laukien Prize in 2014,the Protein Society Young Investigator award in 2012,and the American Chemical Society’s Pure Chemistry award in 2003.
Robert William Carpick is a Canadian mechanical engineer. He is currently director of diversity,equity,and inclusion and John Henry Towne Professor in the Department of Mechanical Engineering and Applied Mechanics at the University of Pennsylvania. He is best known for his work in tribology,particularly nanotribology.
References
- ↑ "AWIS Member Spotlight: Helen Greenwood Hansma, PhD". AWIS. January 18, 2023.
- ↑ "Helen Hansma".
- ↑ Hansma, Helen Greenwood (2022). "DNA and the origins of life in micaceous clay". Biophysical Journal. 121 (24): 4867–4873. Bibcode:2022BpJ...121.4867H. doi: 10.1016/j.bpj.2022.08.032 . PMC 9808538 . PMID 36130604.
- ↑ Satow, Y.; Hansma, H. G.; Kung, C. (1976). "The effect of sodium on "Paranoiac"—A membrane mutant of Paramecium". Comparative Biochemistry and Physiology A. 54 (3): 323–329. doi:10.1016/s0300-9629(76)80120-x. PMID 5223.
- ↑ Grant, James Rodman, Mark Courtney, Sam Scheiner, Carter Kimsey, Rita Teutonico, Alan Tessier atessier, Sally O’Connor soconnor. "Funding Opportunities at the National Science Foundation – ppt download". slideplayer.com.
{{cite web}}: CS1 maint: multiple names: authors list (link) - ↑ "Life Imitates Mica". The Current. September 20, 2022.
- ↑ "Helen Hansma".
- ↑ "NSF Award Search: Award # 9018846 – Sequencing DNA with the Atomic Force Microscope". www.nsf.gov.
- ↑ "NSF Award Search: Award # 9982743 – New Applications for Scanning Probe Microscopy of Biomaterials". www.nsf.gov.
- ↑ "Helen Greenwood Hansma – Google Scholar".
- ↑ "Dr Helen Greenwood Hansma – Energy: A Clue to the Origins of Life • scipod.global". 25 May 2022.
- ↑ Hansma, Helen G.; Sinsheimer, Robert L.; Li, Min-Qian; Hansma, Paul K. (1992). "Atomic force microscopy of single-and double-stranded DNA". Nucleic Acids Research. 20 (14): 3585–3590. doi: 10.1093/nar/20.14.3585 . PMC 334005 . PMID 1386422.
- ↑ Hansma, Helen G (October 25, 2001). "SURFACE BIOLOGY OF DNA BY ATOMIC FORCE MICROSCOPY". Annual Review of Physical Chemistry. 52 (1): 71–92. Bibcode:2001ARPC...52...71H. doi:10.1146/annurev.physchem.52.1.71. PMID 11326059.
- ↑ Bezanilla, M.; Drake, B.; Nudler, E.; Kashlev, M.; Hansma, P. K.; Hansma, H. G. (December 1, 1994). "Motion and enzymatic degradation of DNA in the atomic force microscope". Biophysical Journal. 67 (6): 2454–2459. Bibcode:1994BpJ....67.2454B. doi:10.1016/S0006-3495(94)80733-7. PMC 1225630 . PMID 7696484. S2CID 40517547.
- 1 2 Hansma, H. G.; Golan, R.; Hsieh, W.; Lollo, C. P.; Mullen-Ley, P.; Kwoh, D. (1998). "DNA condensation for gene therapy as monitored by atomic force microscopy". Nucleic Acids Research. 26 (10): 2481–2487. doi: 10.1093/nar/26.10.2481 . PMC 147577 . PMID 9580703.
- ↑ Golan, Roxana; Pietrasanta, Lía I.; Hsieh, Wan; Hansma, Helen G. (October 1, 1999). "DNA Toroids: Stages in Condensation". Biochemistry. 38 (42): 14069–14076. doi:10.1021/bi990901o. PMID 10529254.
- ↑ Hansma, Helen G.; Sinsheimer, Robert L.; Groppe, Jay; Bruice, Thomas C.; Elings, Virgil; Gurley, Gus; Bezanilla, Magdalena; Mastrangelo, Iris A.; Hough, Paul V. C.; Hansma, Paul K. (July 25, 1993). "Recent advances in atomic force microscopy of DNA: Recent advances in AFM of DNA". Scanning. 15 (5): 296–299. doi:10.1002/sca.4950150509. PMID 8269178.
- ↑ Bezanilla, Magdalena; Manne, Srinivas; Laney, Daniel E.; Lyubchenko, Yuri L.; Hansma, Helen G. (February 25, 1995). "Adsorption of DNA to Mica, Silylated Mica, and Minerals: Characterization by Atomic Force Microscopy". Langmuir. 11 (2): 655–659. doi:10.1021/la00002a050.
- ↑ Murray, M N; Hansma, H G; Bezanilla, M; Sano, T; Ogletree, D F; Kolbe, W; Smith, C L; Cantor, C R; Spengler, S; Hansma, P K (May 25, 1993). "Atomic force microscopy of biochemically tagged DNA". Proceedings of the National Academy of Sciences. 90 (9): 3811–3814. Bibcode:1993PNAS...90.3811M. doi: 10.1073/pnas.90.9.3811 . PMC 46395 . PMID 8483898.
- ↑ Hansma, H. G.; Laney, D. E.; Bezanilla, M.; Sinsheimer, R. L.; Hansma, P. K. (May 1, 1995). "Applications for atomic force microscopy of DNA". Biophysical Journal. 68 (5): 1672–1677. Bibcode:1995BpJ....68.1672H. doi:10.1016/S0006-3495(95)80343-7. PMC 1282069 . PMID 7612809.
- ↑ Hansma, H. G.; Laney, D. E. (April 1, 1996). "DNA binding to mica correlates with cationic radius: assay by atomic force microscopy". Biophysical Journal. 70 (4): 1933–1939. Bibcode:1996BpJ....70.1933H. doi:10.1016/S0006-3495(96)79757-6. PMC 1225162 . PMID 8785352.
- ↑ Hansma, Helen G.; Hansma, Paul K. (June 24, 1993). Keller, Richard A. (ed.). Potential applications of atomic force microscopy of DNA to the human genome project. Advances in DNA Sequencing Technology. Vol. 1891. SPIE. pp. 66–70. doi:10.1117/12.146705. S2CID 121508883.
- ↑ Hansma, P. K.; Gaub, H. E.; Edmundson, A. B.; Weisenhorn, A. L.; Hansma, H. G. (1991). "Atomic force microscopy: Seeing molecules of lipid and immunoglobulin". Clinical Chemistry. 37 (9): 1497–1501. doi:10.1093/clinchem/37.9.1497. PMID 1893574.
- ↑ Radmacher, M.; Goettgens, B. M.; Tillmann, R. W.; Hansma, H. G.; Hansma, P. K.; Gaub, H. E.; Hansma, P. K. (1991). "Morphology of Polymerized Membranes on an Amorphous Substrate at Molecular Resolution by AFM". AIP Conference Proceedings. Vol. 241. pp. 144–153. doi:10.1063/1.41432.
- ↑ Hansma, Helen Greenwood (July 25, 2014). Asakura, Tetsuo; Miller, Thomas (eds.). Biotechnology of Silk. Springer Netherlands. pp. 123–136. doi:10.1007/978-94-007-7119-2_7.
- ↑ Oroudjev, Emin; Hayashi, Cheryl Y.; Soares, Jason; Arcidiacono, Steven; Fossey, Stephen A.; Hansma, Helen G. (January 25, 2002). "Nanofiber Formation in Spider Dragline-Silk as Probed by Atomic Force Microscopy and Molecular Pulling". MRS Online Proceedings Library. 738: G10.4. doi:10.1557/PROC-738-G10.4.
- ↑ Becker, Nathan; Oroudjev, Emin; Mutz, Stephanie; Cleveland, Jason P.; Hansma, Paul K.; Hayashi, Cheryl Y.; Makarov, Dmitrii E.; Hansma, Helen G. (April 25, 2003). "Molecular nanosprings in spider capture-silk threads". Nature Materials. 2 (4): 278–283. Bibcode:2003NatMa...2..278B. doi:10.1038/nmat858. PMID 12690403. S2CID 7419692.
- ↑ Oroudjev, E.; Soares, J.; Arcidiacono, S.; Thompson, J. B.; Fossey, S. A.; Hansma, H. G. (April 30, 2002). "Segmented nanofibers of spider dragline silk: Atomic force microscopy and single-molecule force spectroscopy". Proceedings of the National Academy of Sciences. 99 (suppl_2): 6460–6465. Bibcode:2002PNAS...99.6460O. doi: 10.1073/pnas.082526499 . PMC 128550 . PMID 11959907.
- ↑ Auerbach, Ilene D.; Sorensen, Cody; Hansma, Helen G.; Holden, Patricia A. (July 25, 2000). "Physical Morphology and Surface Properties of Unsaturated Pseudomonas putida Biofilms". Journal of Bacteriology. 182 (13): 3809–3815. doi:10.1128/JB.182.13.3809-3815.2000. PMC 94554 . PMID 10850998.
- ↑ R. E. Steinberger; Allen, A. R.; Hansma, H. G.; P. A. Holden (2002). "Elongation Correlates with Nutrient Deprivation in Pseudomonas aeruginosa-Unsaturated Biofilms". Microbial Ecology. 43 (4): 416–423. Bibcode:2002MicEc..43..416S. doi:10.1007/s00248-001-1063-z. JSTOR 4287616. PMID 12043001.
- ↑ Hansma, Helen Greenwood; Oroudjev, Emin (2010). "Atomic Force Microscopy of Biomaterials, Mica, and the Origins of Life". Microscopy Today. 18 (6): 16–20. doi: 10.1017/S1551929510000970 .
- ↑ Hansma, Helen Greenwood (January 25, 2009). "Could Life Originate between Mica Sheets?: Mechanochemical Biomolecular Synthesis and the Origins of Life". MRS Online Proceedings Library. 1185: 1185. doi:10.1557/PROC-1185-II03-15.
- ↑ "The Secret of Life May Be As Simple As What Happens Between the Sheets--Mica Sheets".
- ↑ Hansma, Helen Greenwood (August 25, 2013). "Possible origin of life between mica sheets: does life imitate mica?". Journal of Biomolecular Structure and Dynamics. 31 (8): 888–895. doi:10.1080/07391102.2012.718528. PMC 3725661 . PMID 22963072.
- ↑ Hansma, Helen Greenwood (December 1, 2014). "The Power of Crowding for the Origins of Life". Origins of Life and Evolution of Biospheres. 44 (4): 307–311. Bibcode:2014OLEB...44..307H. doi:10.1007/s11084-014-9382-5. PMID 25585799. S2CID 254892113.
- ↑ Hansma, Helen Greenwood (June 25, 2017). "Better than Membranes at the Origin of Life?". Life. 7 (2): 28. Bibcode:2017Life....7...28H. doi: 10.3390/life7020028 . PMC 5492150 . PMID 28632159.
- ↑ Hansma, Helen Greenwood (December 25, 2020). "Mechanical Energy before Chemical Energy at the Origins of Life?". Sci. 2 (4): 88. doi: 10.3390/sci2040088 .
- ↑ "Did life get its start in micaceous clay?".