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The interaction of proteins with surfaces is a key phenomenon in many applications, but current understanding of the biophysics involved is lacking. At present, rational design of such emerging technologies is difficult as no methods or theories exist that correctly predict how surfaces influence protein behavior. Using molecular simulation and a coarse-grain model, this study illustrates for the first time that stability of proteins on surfaces can be correlated with tertiary structural elements for alpha-helical, orthogonal-bundle proteins. Results show that several factors contribute to stability on surfaces including the nature of the loop region where the tether is placed and the ability of the protein to freely rotate on the surface. A thermodynamic analysis demonstrates that surfaces stabilize proteins entropically and that any destabilization is an enthalpic effect. Moreover, the entropic effects are concentrated on the unfolded state of the protein while the ethalpic effects are focused on the folded state. [ABSTRACT FROM AUTHOR]

Circulating tumor cells (CTCs) are an important biomarker for various types of cancers. As CTCs are extremely rare in the bloodstream, the accurate analysis and efficient separation of CTCs is a challenging task. In order to develop new diagnostic approaches for cancer research, understanding the functional characteristics of biomolecules at the single-molecule level in individual cancer cells is required. Meanwhile, microfluidic platforms have emerged as a promising technology for analyzing single molecules and single cells. In this review, we discuss some label-free techniques for biomolecule detection and highlight some reports that have employed combined label-free techniques with microfluidics for individual molecule or cancer cell analysis. Finally, we offer our perspective of the integration of label-free techniques with microfluidic technology on future applications. • Label-free techniques were utilized for biomolecules detection. • Microfluidic were utilized for analyzing single molecules and single cells. • Analysis of biomolecule and CTCs based on label-free techniques with microfluidic. [ABSTRACT FROM AUTHOR]

Solution-state NMR typically requires 100 μM to 1 mM samples. This limitation prevents applications to mass-limited and aggregationprone target molecules. Photochemically induced dynamic nuclear polarization was adapted to data collection on low-concentration samples by radiofrequency gating, enabling rapid 1D NMR spectral acquisition on aromatic amino acids and proteins bearing aromatic residues at nanomolar concentration, i.e., a full order of magnitude below other hyperpolarization techniques in liquids. Both backbone H1-C13 and side-chain resonances were enhanced, enabling secondary and tertiary structure analysis of proteins with remarkable spectral editing, via the 13C PREPRINT pulse sequence. Laser-enhanced 2D NMR spectra of 5 μM proteins at 600 MHz display 30-fold better S/N than conventional 2D data collected at 900 MHz. Sensitivity enhancements achieved with this technology, denoted as low-concentration photo- CIDNP (LC-photo-CIDNP), depend only weakly on laser intensity, highlighting the opportunity of safer and more cost-effective hypersensitive NMR applications employing low-power laser sources. [ABSTRACT FROM AUTHOR]

For many proteins, phosphorylation regulates their interaction with other biomolecules. Herein, we describe an unexpected phenomenon whereby phosphate groups are transferred non-enzymatically from one interaction partner to the other within a binding interface upon activation in the gas phase. Providing that a high affinity exists between the donor and acceptor sites, this phosphate transfer is very efficient and the phosphate groups only ligate to sites in proximity to the binding region. Consequently, such phosphate-transfer reactions may define with high precision the binding site between a phosphoprotein and its binding partner, as well as reveal that the binding site in this system is retained in the phase transfer from solution to the gas phase. [ABSTRACT FROM AUTHOR]

Paper-based fluorescence resonance energy transfer assay (FRET) is gaining great interest in detecting macro-biological molecule. It is difficult to achieve conveniently and fast detection for macro-biological molecule. Herein, a graphene oxide (GO)-based paper chip (glass fiber) integrated with fluorescence labeled single-stranded DNA (ssDNA) for fast, inexpensive and direct detection of biological macromolecules (proteins and nucleic acids) has been developed. In this paper, we employed the Cy3/FAM-labeled ssDNA as the reporter and the GO as quencher and the original glass fiber paper as data acquisition substrates. The chip which was designed and fabricated by a cutting machine is a miniature biosensor that monitors fluorescence recovery from resonance energy transfer. The hybridization assays and fluorescence detection were all simplified, and the surface of the chip did not require immobilization or washing. A Nikon Eclipse was employed as excited resource and a commercial digital camera was employed for capturing digital images. This paper-based microfluidics chip has been applied in the detection of proteins and nucleic acids. The biosensing capability meets many potential requirements for disease diagnosis and biological analysis. [ABSTRACT FROM AUTHOR]

Site-directed (gene) mutagenesis has been the most useful method available for the conversion of one amino acid residue of a given protein into another. Until relatively recently, this strategy was limited to the twenty standard amino acids. The ongoing maturation of stop codon suppression and related technologies for unnatural amino acid incorporation has greatly expanded access to nonstandard amino acids by expanding the scope of the translational apparatus. However, the necessity for translation of genetic changes restricts the diversity of residues that may be incorporated. Herein we highlight an alternative approach, termed post-expression mutagenesis, which operates at the level of the very functional biomolecules themselves. Using the lens of retrosynthesis, we highlight prospects for new strategies in protein modification, alteration, and construction which will enable protein science to move beyond the constraints of the 'translational filter' and lead to a true synthetic biology. [ABSTRACT FROM AUTHOR]

Primary free radicals generated under oxidative stress in cells and tissues produce a cascade of reactive secondary radicals, which attack biomolecules with efficiency determined by the reaction rate constants and target concentration. Proteins are prominent targets because they constitute the bulk of the organic content of cells and tissues and react readily with many of the secondary radicals. The reactions commonly lead to the formation of carbon-centered radicals, which generally convert in vivo to peroxyl radicals and finally to semistable hydroperoxides. All of these intermediates can initiate biological damage. This article outlines the advantages of the application of ionizing radiations to studies of radicals, with particular reference to the generation of desired radicals, studies of the kinetics of their reactions and correlating the results with events in biological systems. In one such application, formation of protein hydroperoxides in irradiated cells was inhibited by the intracellular ascorbate and glutathione. [ABSTRACT FROM AUTHOR]

Fabrication of metal-organic frameworks (MOFs) with large apertures triggers a brand-new research area for selective encapsulation of biomolecules within MOF nanopores. The underlying inclusion mechanism is yet to be clarified however. Here we report a molecular dynamics study on the mechanism of protein encapsulation in MOFs. Evaluation for the binding of amino acid side chain analogues reveals that van der Waals interaction is the main driving force for the binding and that guest size acts as a key factor predicting protein binding with MOFs. Analysis on the conformation and thermodynamic stability of the miniprotein Trp-cage encapsulated in a series of MOFs with varying pore apertures and surface chemistries indicates that protein encapsulation can be achieved via maintaining a polar/nonpolar balance in the MOF surface through tunable modification of organic linkers and Mg-O chelating moieties. Such modifications endow MOFs with a more biocompatible confinement. This work provides guidelines for selective inclusion of biomolecules within MOFs and facilitates MOF functions as a new class of host materials and molecular chaperones. [ABSTRACT FROM AUTHOR]

Most of the protein-based diseases are caused by anomalies in the functionality and stability of these molecules. Experimental and theoretical studies of the conformational dynamics of proteins are becoming in this respect essential to understand the origin of these anomalies. However, a description of the conformational dynamics of proteins based on mechano-energetic principles still remains elusive because of the intrinsic high flexibility of the peptide chains, the participation of weak noncovalent interactions, and the role of the ubiquitous water solvent. In this work, the conformational dynamics of trialanine dissolved in water (D2O) is investigated through Molecular Dynamics (MD) simulations combined with instantaneous normal modes (INMs) analysis both at equilibrium and after the vibrational excitation of the C-terminal amide I mode. The conformational equilibrium between a and pPII conformers is found to be altered by the intramolecular relaxation of the amide I mode as a consequence of the different relaxation pathways of each conformer which modify the amount of vibrational energy stored in the torsional motions of the tripeptide, so the a ? pPII and pPII ? a conversion rates are increased differently. The selectivity of the process comes from the shifts of the vibrational frequencies with the conformational changes that modify the resonance conditions driving the intramolecular energy flows. [ABSTRACT FROM AUTHOR]

The recent synthetic development of a variety of nanoparticles has led to their widespread application in diagnostics and therapeutics. In particular, the controlled size and shape of nanoparticles precisely determine their unique chemical and physical properties, which is highly attractive for accurate analysis of given systems. In addition to efforts toward controlling the synthesis and properties of nanoparticles, the surface functionalization of nanoparticles with biomolecules has been intensively investigated since the mid-1990s. The complicated yet programmable properties of biomolecules have proved to substantially enhance and enrich the novel functions of nanoparticles to achieve 'smart' nanoparticle materials. In this review, the advances in chemical functionalization of four types of representative nanoparticle with DNA and protein molecules in the past five years are critically reviewed, and their future trends are predicted. [ABSTRACT FROM AUTHOR]

Dynamics can provide deep insights into the functional mechanisms of proteins and protein complexes. For large protein complexes such as GroEL/GroES with more than 8,000 residues, obtaining a fine-grained all-atom description of its normal mode motions can be computationally prohibitive and is often unnecessary. For this reason, coarse-grained models have been used successfully. However, most existing coarse-grained models use extremely simple potentials to represent the interactions within the coarse-grained structures and as a result, the dynamics obtained for the coarse-grained structures may not always be fully realistic. There is a gap between the quality of the dynamics of the coarse-grained structures given by all-atom models and that by coarse-grained models. In this work, we resolve an important question in protein dynamics computations—how can we efficiently construct coarse-grained models whose description of the dynamics of the coarse-grained structures remains as accurate as that given by all-atom models? Our method takes advantage of the sparseness of the Hessian matrix and achieves a high efficiency with a novel iterative matrix projection approach. The result is highly significant since it can provide descriptions of normal mode motions at an all-atom level of accuracy even for the largest biomolecular complexes. The application of our method to GroEL/GroES offers new insights into the mechanism of this biologically important chaperonin, such as that the conformational transitions of this protein complex in its functional cycle are even more strongly connected to the first few lowest frequency modes than with other coarse-grained models. [ABSTRACT FROM AUTHOR]

The equations of state, adsorption isotherms and functions of the distribution of protein molecules in liquid interfacial layers with respect to molar area and the equations for their viscoelastic behavior are presented. This theory was used to determine the adsorption characteristics of β-casein and β-lactoglobulin at water/oil interfaces. The experimental results are shown to be describable quite adequately by the proposed theory with consistent model parameters. The data analysis demonstrated that the β-casein molecule adsorbed at equilibrium conditions is more unfolded as compared with dynamic conditions, and this fact causes the significant increase of the adsorption equilibrium constant. The theory assumes the adsorption of protein molecules from the aqueous solution and a competitive adsorption of alkane molecules from the alkane phase. The comparison of the experimental equilibrium interfacial tension isotherms for β-lactoglobulin at the solution/hexane interface with data calculated using the proposed theoretical model demonstrates that the assumption of a competitive adsorption is essential, and the influence of the hexane molecules on the shape of the adsorption isotherm does in fact exist. [ABSTRACT FROM AUTHOR]

Protein molecules work as a whole, so that any local perturbation may resonate on the entire structure: allostery deals with this general property of protein molecules. It is worth noting a perturbation does not necessarily involve a conformational change but, more generally, it travels across the structure as an ‘energy signal’. The atomic interactions within the network provide the structural support for this ‘signaling highway’. Network descriptors, capturing network signaling efficiency, explain allostery in terms of signal transmission. In this review we will survey the key applications of graph theory to protein allostery. The complex network approach introduces a new perspective in biochemistry; as for applications, the development of new drugs relying on allosteric effects (allo-network drugs) represents a promising avenue of contact network formalism. [ABSTRACT FROM AUTHOR]

Over the past decade, great developments in optical microscopy have made this technology increasingly compatible with biological studies. Fluorescence microscopy has especially contributed to investigating the dynamic behaviors of live specimens and can now resolve objects with nanometer precision and resolution due to super-resolution imaging. Additionally, single particle tracking provides information on the dynamics of individual proteins at the nanometer scale both in vitro and in cells. Complementing advances in microscopy technologies has been the development of fluorescent probes. The quantum dot, a semi-conductor fluorescent nanoparticle, is particularly suitable for single particle tracking and super-resolution imaging. This article overviews the principles of single particle tracking and super resolution along with describing their application to the nanometer measurement/observation of biological systems when combined with quantum dot technologies. [ABSTRACT FROM AUTHOR]

Wereport a versatile analysis platform, based on a set of nanogapelectrodes, for the manipulation and sensing of biomolecules, as demonstratedhere for low-copy number protein detection. An array of Ti nanogapelectrode with sub-10 nm gap size function as templates for alternatingcurrent dielectrophoresis-based molecular trapping, hot spots forsurface-enhanced Raman spectroscopy as well as electronic measurements,and fluorescence imaging. During molecular trapping, recorded Ramanspectra, conductance measurements across the nanogaps, and fluorescenceimaging show unambiguously the presence and characteristics of thetrapped proteins. Our platform opens up a simple way for multifunctionallow-concentration heterogeneous sample analysis without the need fortarget preconcentration. [ABSTRACT FROM AUTHOR]

Abstract: In this study, a microfluidic platform was developed to generate single layer, linear array of microbeads for multiplexed high-throughput analysis of biomolecules. The microfluidic device is comprised of eight microbead-trapping units, where microbeads were immobilized in a linear array format by the exertion of a negative pressure in the control channel connected to each sieving microstructure. Multiplexed assays were achieved by using a mixture of different spectrally-encoded microbeads functionalized with specific probes, followed by on-chip reaction and detection. The microfluidic-based microbeads array platform was employed for multiplexed analysis of DNA and proteins, as demonstrated by the simultaneous discrimination of four HPV genotypes and the parallel detection of six different proteins. Compared with the off-chip protocols, the on-chip analysis exhibited better reaction efficiency, higher sensitivity and wider linear detection range. Visual inspection and identification of functionalized microbeads were facilitated by the single layer arrangement of microbeads so that accurate data acquisition can be performed during the detection process. [Copyright &y& Elsevier]

A blended approach encompassing problem-based learning (PBL) and structured inquiry was used in this laboratory exercise based on the congenital disease Osteogenesis imperfecta (OI), to introduce commonly used techniques in biomolecular analysis within a clinical context. During a series of PBL sessions students were presented with several scenarios involving a 2 year old child, who had experienced numerous fractures. Key learning goals related to both the theory and practical aspects of the course, covering biomolecular analysis and functional genomics, were identified in successive PBL sessions. The laboratory exercises were conducted in 3 hour blocks over six weeks, focused firstly on protein analysis, followed by nucleic acids. Students isolated collagen from normal and OI affected fibroblast cultures. Analysis by SDS-PAGE demonstrated α1 and α2 of collagen Type I chains at approximately 95 kDa and 92 kDa, respectively. Subtle differences in protein mobility between the control and OI samples were observed by some students, but most considered it inconclusive as a diagnostic tool. The nucleic acid module involved isolation of RNA from OI affected fibroblasts. The RNA was reverse transcribed and used as template to amplify a 354 bp COL1A1 fragment. Students were provided with the sequence of the OI affected COL1A1 PCR product aligned with the normal COL1A1 sequence, allowing identification of the mutation, as the substitution of Arg for Gly976 of the triple helical region. Our experience with student cohorts over several years is that presentation of this laboratory exercise within a relevant clinical context, and the opportunity for active engagement with the experimental procedures via PBL sessions, supported the learning of basic theory and practical techniques of biomolecular analysis. © 2013 by The International Union of Biochemistry and Molecular Biology 41(2):103-109, 2013 [ABSTRACT FROM AUTHOR]

Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) provides the highest mass resolving power and mass measurement accuracy for unambiguous identification of biomolecules. Previously, the highest-mass protein for which FTICR unit mass resolution had been obtained was 115 kDa at 7 T. Here, we present baseline resolution for an intact 147.7 kDa monoclonal antibody (mAb), by prior dissociation of noncovalent adducts, optimization of detected total ion number, and optimization of ICR cell parameters to minimize space charge shifts, peak coalescence, and destructive ion cloud Coulombic interactions. The resultant long ICR transient lifetime (as high as 20 s) results in magnitude-mode mass resolving power of 420?000 at m/z 2?593 for the 57+ charge state (the highest mass for which baseline unit mass resolution has been achieved), auguring for future characterization of even larger intact proteins and protein complexes by FTICR MS. We also demonstrate up to 80% higher resolving power by phase correction to yield an absorption-mode mass spectrum. [ABSTRACT FROM AUTHOR]

We show that the weak signal that remains after 13C-detected experiments (the 13C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA-(CO)NNH, into a single pulse sequence that makes use of two receivers in parallel. In cases where the sensitivity is not limiting, such as applications to small proteins, the inclusion of the projection-reconstruction method permits the recording of both spectra in only 15 mm. High-quality data sets for the 143 residue nuclease A inhibitor (2°C, correlation time 17.5 ns) were obtained in 3 h, illustrating the utility of the method even in studies of moderately sized proteins. [ABSTRACT FROM AUTHOR]

Abstract: “Label-free” biomolecule sensors for detection of inflammatory cardiovascular biomarker associated with vulnerable coronary vascular plaque rupture were designed and fabricated using micro- and nanotextured polystyrene (PS) polymer structures that functioned as sensing elements coupled with electronic measurement equipment. We demonstrated that scaling down the surface texturing from the micro- to the nanoscale enhances the amplitude of the measured detected signal strength. We believe that the nanoscale fiber morphology provides size-matched spaces for trapping and immobilizing the protein biomolecule, resulting in improved detection signal strength. We selected PS as the model system and demonstrated the detection of human serum C-reactive protein. We employed these findings in designing a platform “lab-on-a-chip” protein sensor. Comparative studies were performed on PS textured surfaces of two different surface features: a PS microsphere mat and an electrospun PS nanofiber matrix. From the Clinical Editor: In this study, nanotechnology-based biosensors for vulnerable coronary vascular plaque rupture were designed and fabricated using micro- and nanotextured polystyrene polymer structures. The authors demonstrated that scaling down the surface texturing from the micro- to the nanoscale enhances the sensitivity of this detection method. [ABSTRACT FROM AUTHOR]

Ultrasensitive detection of proteins is of great importance to proteomics studies. We report here a method to enhance detection sensitivity in surface plasmon resonance (SPR) spectroscopy by coupling a polymerization initiator to a biospecific interaction and inducing inline atom transfer radical polymerization (AThP) for amplifying SPR response. Bacterial cholera toxin (CI) is chosen as the model protein that has been covalently immobilized on the surface for demonstrating the principle. The specific recognition is achieved by use of biotinylated anti-CF, which allows initiators nith a biotin tag to be fixed at the protein binding site through a neutravidin bridge and triggers the localized growth of polymer brushes of poly-(hydroxyl-ethyl methacrylate) (PHEMA) via an ATRP mechanism. To further enhance the signal, a second ATRP reaction is conducted that takes advantage of the hydroxyl groups of PHEMA brushes from the first step to form hypethranched polymers onto the sensing surface. The two consecutive ATRP steps significantly improve SPR detection, allowing low amounts of CF that yield no direct measurement to be quantified with large signals. The resulting polymer film has been characterized by optical and atomic force microscopy. Ascorbic acid (AA) is employed as deoxygen reagent in the catalyst mixture that effectively suppresses oxygen interference, shortening the reaction time and making it possible for applying this ATRP approach to flow injection based SPR detection. A calibration curve of PHEMA amplification for CF detection based on suiface coverage has been obtained that displays a correlation in a range from 8.23 x 10-15 to 3.61 x 10-12 mol/cm2 with a limit of detection of 6.27 x 10-15 mol/cm2. The versatile biotin-neutravidin interaction used here should allow adaptation of ATRP enhancement to many other systems that include DNA, RNA, peptides, and carbohydrates, opening new avenues for ultrasensitive analysis of biomolecules with flow-injection assay and SPR spectroscopy. [ABSTRACT FROM AUTHOR]

It is well known that most proteins and many other biomolecules fluoresce when illuminated with UV radiation, but it is also commonly accepted that utilizing this property to detect protein crystals in crystallization setups is limited by the opacity of the materials used to contain and seal them. For proteins, this fluorescence property arises primarily from the presence of tryptophan residues in the sequence. Studies of protein crystallization results in a variety of setup configurations show that the opacity of the containment hardware can be overcome at longer excitation wavelengths, where typical hardware materials are more transparent in the UV, by the use of a powerful UV-light source that is effective in excitation even though not at the maximum of the excitation response. The results show that under these circumstances UV evaluation of crystallization trials and detection of biomolecular crystals in them is not limited by the hardware used. It is similarly true that a deficiency in tryptophan or another fluorescent component that limits the use of UV light for these purposes can be effectively overcome by the addition of fluorescent prostheses that bind to the biomolecule under study. The measurements for these studies were made with a device consisting of a potent UV-light source and a detection system specially adapted (i) to be tunable via a motorized and software-controlled absorption-filter system and (ii) to convey the excitation light to the droplet or capillary hosting the crystallization experiment by quartz-fibre light guides. [ABSTRACT FROM AUTHOR]

A new trifunctional probe, assembled using a cleavable linker, is useful for efficient enrichment and detection of alkynyl sugar-tagged biomolecules. [ABSTRACT FROM AUTHOR]

Motivation: Lipid, an essential class of biomolecules, is receiving increasing attention in the research community, especially with the development of analytical technique like mass spectrometry. Gene Ontology (GO) is the de facto standard function annotation scheme for gene products. Identification of both explicit and implicit lipid-related GO terms will help lipid research in many ways, e.g. assigning lipid function in protein function prediction.Results: We have constructed a Web site ‘LipidGO’ that facilitates browsing and searching lipid-related GO terms. An expandable hierarchical GO tree is constructed that allows users to find lipid-related GO terms easily. To support large-scale analysis, a user is able to upload a list of gene products or a list of GO terms to find out which of them is lipid related. Finally, we demonstrate the usefulness of ‘LipidGO’ by two applications: (i) identifying lipid-related gene products in model organisms and (ii) discovering potential novel lipid-related molecular functionsAvailability and implementation: LipidGO is available at http://compbio.ddns.comp.nus.edu.sg/%7elipidgo/index.php.Contact: wongls@comp.nus.edu.sgSupplementary Information: Supplementary data are available at Bioinformatics online. [ABSTRACT FROM AUTHOR]

Modeling of biomolecular systems plays an essential role in understanding biological processes, such as ionic flow across channels, protein modification or interaction, and cell signaling. The continuum model described by the Poisson– Boltzmann (PB)/Poisson–Nernst–Planck (PNP) equations has made great contributions towards simulation of these processes. However, the model has shortcomings in its commonly used form and cannot capture (or cannot accurately capture) some important physical properties of the biological systems. Considerable efforts have been made to improve the continuum model to account for discrete particle interactions and to make progress in numerical methods to provide accurate and efficient simulations. This review will summarize recent main improvements in continuum modeling for biomolecular systems, with focus on the size-modified models, the coupling of the classical density functional theory and the PNP equations, the coupling of polar and nonpolar interactions, and numerical progress. [ABSTRACT FROM AUTHOR]

The article evaluates several life science technology products including the BiacoreT200 system for interaction analysis by GE Healthcare, the Fe-NTA Phosphopeptide Enrichment Kit by Thermo Scientific, and a mass spectrometry protein standard by OriGene Technologies.

The chlorosome envelope of Chlorobaculum tepidum contains 10 proteins that belong to four structural motif families. A previous mutational study (N.-U. Frigaard, H. Li, K. J. Milks, and D. A. Bryant, J. Bacteriol. 186:646-653, 2004) suggested that some of these proteins might have redundant functions. Six multilocus mutants were constructed to test the effects of eliminating the proteins of the CsmC/CsmD and CsmB/CsmF motif families, and the resulting strains were characterized physiologically and biochemically. Mutants lacking all proteins of either motif family still assembled functional chlorosomes, and as measured by growth rates of the mutant strains, light harvesting was affected only at the lowest light intensities tested (9 and 32 μmol photons m-2 s-1). The size, composition, and biogenesis of the mutant chlorosomes differed from those of wild-type chlorosomes. Mutants lacking proteins of the CsmC/CsmD motif family produced smaller chlorosomes than did the wild type, and the Qy absorbance maximum for the bacteriochlorophyll c aggregates in these chlorosomes was strongly blueshifted. Conversely, the chlorosomes of mutants lacking proteins of the CsmB/CsmF motif family were larger than wild-type chlorosomes, and the Qy absorption for their bacteriochlorophyll c aggregates was redshifted. When CsmH was eliminated in addition to other proteins of either motif family, chlorosomes had smaller diameters. These data show that the chlorosome envelope proteins of the CsmB/CsmF and CsmC/CsmD families play important roles in determining chlorosome size as well as the assembly and supramolecular organization of the bacteriochlorophyll c aggregates within the chlorosome. [ABSTRACT FROM AUTHOR]