In development for two years, Eat Me Guilt Free's new and improved formula has less sugar, is non-GMO and uses modified atmosphere packaging to exclude unnecessary preservatives.

The new formula has mass appeal for consumers looking to kick-start their morning, power through an afternoon slump, get ready to exercise and fuel late-night contests. 

Aware that consumers prioritize clean, accessible and convenient ways to up protein intake and energy, Clean Simple Eats has crafted the a solution. Designed for those who value transparency in their nutrition choices, these beverages offer a refreshing approach to fitness fuel. 

EverGrain Ingredients, a barley fiber and protein ingredient company backed by Anheuser-Busch InBev, offers ingredients that aim to enable a new benchmark for limited water use, emissions, and land use while ensuring better nutrition and taste. 

Power Life™ by Tony Horton launched its latest flavor of protein powders: Strawberry Vanilla High Impact Whey Protein and Strawberry Vanilla High Impact Plant Protein.

Crafted with invigorating organic ingredients, each 12oz ready-to-drink AWAKE+PROTEIN latte is fortified with 10g of plant-powered protein and 200mg of Lion's Mane mushroom extract, a nootropic clinically proven to support cognitive function.

Döhler will dedicate substantial fermentation capacity to the production of Superbrewed Food’s patented Postbiotic Protein ingredient, which will support product launches in 2024 in several food categories in the United States with multiple consumer package foods companies.

Whether consumers are preparing for a workout, seeking a post-exercise recovery drink, or need a convenient and nutritious boost on the go, these multi-functional smoothies are formulated to enhance fitness routines. 

Designer Wellness, a source for nutrient-filled protein powders and other wellness products, introduced Designer Smoothie, a shelf stable and portable protein fruit smoothie that is made with real fruit, contains 12g of whey protein isolate, is all natural, gluten free, has 100% BPA free packaging and contains no sugar added.

CytoGUARD® OX-WST natural antioxidants are part of the company’s portfolio of natural preservation solutions, which include ingredients providing food safety and shelf life extension. 

Prepared Foods Chief Editor Bob Garrison talks protein with Dr. Baljit Ghotra, co-CEO and co-founder of EQUII Foods, a San Francisco Bay-area start-up whose Equii retail and foodservice breads and bread mixes boast two times more protein, 30% fewer carbs, and 50% less sugar compared to other leading brands.

EQUII created a complete protein flour using fermentation, with the launch of its flagship Bread products last year. EQUII’s goal is to disrupt age-old fermentation methods with modern day innovation, combined with culinary art to make animal-free products that deliver great taste and complete protein.

Made with less sugar than most chocolate bars with a similar taste, Oobli chocolate bars are gut- and diabetic-friendly.

Surthrival launched Black Walnut Protein Powder, a sustainable, wild-crafted protein powder sourced from black walnuts collected by foragers in the American Midwest. 

Each new bar is packed with 15g of protein from peanuts or almonds, pea protein and other wholesome ingredients that deliver a satisfying protein boost. 

Dedicated to providing high-quality protein that helps consumers better themselves daily, these new snackable varieties combine BUILT™ protein and balanced macros with a playful experience across texture, flavor, consistency, size, and shape.

Alani Protein Bars are offered in three nostalgic flavors including Peanut Butter & Jelly, Rocky Road and Caramel Crunch. Each protein bar is packed with up to 17g of protein with 220 calories or less.

G FUEL Protein Puffs are performance-based corn snacks that boasts 17g of protein per 1oz bag. 

Each bar delivers 20g of protein per serving. They are also gluten free, low sugar and under 200 calories, making them a nutrient-packed alternative to the sugary snacks and desserts that inspired the new flavors.

The new milk chocolate peanut spread is made from six pure ingredients, including premium nuts, high-grade NZMP whey protein and Nutiani’s specialized phospholipid concentrated WPC.

Available in both Buttermilk and Original varieties, the pancake mixes have 15g of protein per serving and can be made by just adding water.

Candy fanatics and protein enthusiasts alike can now enjoy the smooth taste of iconic Reese's peanut butter in a new, better-for-you format with 18g of protein and 3g of sugar.

4th & Heart continues to revolutionize the ways in which consumers integrate ghee into their daily lifestyles with a the decadent protein, energy and collagen WOKE bars.

With the launch of Bone Broth — inspired by soups and stews — Cerebelly is responding to parents' requests for more variety and are now able to offer their children Cerebelly's full portfolio of products more often for a longer period of time throughout key developmental milestones.

The new 10,000-square-foot facility was constructed on ICL’s 19-acre production campus in St. Louis. At full capacity the plant is expected to produce more than 15 million pounds of product each year. 

Soylent's Complete Protein Shakes are made with 30g of complete plant protein, 28 immune supporting vitamins & minerals, zero sugar, 1,000mg Omega-3, 250 calories of slow-burning carbs, and 60% of the daily recommended value of protein.

Using advanced ultrafiltration technology, Nurri's new Milk Shakes retain essential proteins and minerals while delivering a rich, creamy taste with high protein and low sugar. 

Physically active consumers want convenient, protein-packed options to fit into their on-the-go routine. “Plant-powered” ready-to-drink (RTD) and ready-to-mix (RTM) protein beverages are emerging as a perfect solution to fill this niche nutrition category and grow into the mainstream market.

Available in two new flavors, Maple Almond and Honey Pecan, Wheaties Protein is made with hearty nut-clustered whole grain flakes, almonds or pecans, pumpkin seeds and honey or maple syrup.

The latest product innovation showcases the just-baked texture, organic ingredients, and whole grain nutrition that consumers know paired with plant-based protein for that extra boost.

Initially available on soylent.com and amazon.com in both Chocolate and Vanilla, Soylent Complete Protein Powder levels up the protein shake category by offering a nutritious blend.

Through the collaboration, ADM will process and commercialize a portfolio of proprietary ingredients derived from Benson Hill Ultra-High Protein (UHP) soybeans through an exclusive North American licensing partnership.

When it comes to production, similarities exist among alternative and animal protein processes, but several differences occur, particularly around operational footprint, equipment, and water and energy usage.

Clextral’s new technology combines the principle of a shear-cell fibration process and the continuous extrusion process.

It’s no surprise that alternative meat products are popping up everywhere these days. In fact, they have grown so much that Ernst & Young data predicts alternative meat could see 40% market share by volume by 2040 in the United States.

Spent brewers’ grains not only provide a source of energy for a brewery, but can also provide a salable, high-value protein.

The company upcycles food waste to grow mycelium protein.

Gavin Steingo (Princeton University) Title and description TBA A reception will follow.

Mycobacterium tuberculosis can reside and persist in deep tissues; latent tuberculosis can evade immune detection and has a unique mechanism to convert it into active disease through reactivation. M. tuberculosis Rv1421 (MtRv1421) is a hypothetical protein that has been proposed to be involved in nucleotide binding-related metabolism in cell-growth and cell-division processes. However, due to a lack of structural information, the detailed function of MtRv1421 remains unclear. In this study, a truncated N-terminal domain (NTD) of MtRv1421, which contains a Walker A/B-like motif, was purified and crystallized using PEG 400 as a precipitant. The crystal of MtRv1421-NTD diffracted to a resolution of 1.7 Å and was considered to belong to either the C-centered monoclinic space group C2 or the I-centered orthorhombic space group I222, with unit-cell parameters a = 124.01, b = 58.55, c = 84.87 Å, β = 133.12° or a = 58.53, b = 84.86, c = 90.52 Å, respectively. The asymmetric units of the C2 or I222 crystals contained two or one monomers, respectively. In terms of the binding ability of MtRv1421-NTD to various ligands, uridine diphosphate (UDP) and UDP-N-acetylglucosamine significantly increased the melting temperature of MtRv1421-NTD, which indicates structural stabilization through the binding of these ligands. Altogether, the results reveal that a UDP moiety may be required for the interaction of MtRv1421-NTD as a nucleotide-binding protein with its ligand.

Brucella ovis is an etiologic agent of ovine epididymitis and brucellosis that causes global devastation in sheep, rams, goats, small ruminants and deer. There are no cost-effective methods for the worldwide eradication of ovine brucellosis. B. ovis and other protein targets from various Brucella species are currently in the pipeline for high-throughput structural analysis at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), with the aim of identifying new therapeutic targets. Furthermore, the wealth of structures generated are effective tools for teaching scientific communication, structural science and biochemistry. One of these structures, B. ovis leucine-, isoleucine-, valine-, threonine- and alanine-binding protein (BoLBP), is a putative periplasmic amino acid-binding protein. BoLBP shares less than 29% sequence identity with any other structure in the Protein Data Bank. The production, crystallization and high-resolution structures of BoLBP are reported. BoLBP is a prototypical bacterial periplasmic amino acid-binding protein with the characteristic Venus flytrap topology of two globular domains encapsulating a large central cavity containing the peptide-binding region. The central cavity contains small molecules usurped from the crystallization milieu. The reported structures reveal the conformational flexibility of the central cavity in the absence of bound peptides. The structural similarity to other LBPs can be exploited to accelerate drug repurposing.

Porphyromonas gingivalis is a major pathogenic oral bacterium that is responsible for periodontal disease. It is linked to chronic periodontitis, gingivitis and aggressive periodontitis. P. gingivalis exerts its pathogenic effects through mechanisms such as immune evasion and tissue destruction, primarily by secreting various factors, including cysteine proteases such as gingipain K (Kgp), gingipain R (RgpA and RgpB) and PrtH (UniProtKB ID P46071). Virulence proteins comprise multiple domains, including the pro-peptide region, catalytic domain, K domain, R domain and DUF2436 domain. While there is a growing database of knowledge on virulence proteins and domains, there was no prior evidence or information regarding the structure and biological function of the well conserved DUF2436 domain. In this study, the DUF2436 domain of PrtH from P. gingivalis (PgDUF2436) was determined at 2.21 Å resolution, revealing a noncanonical β-jelly-roll sandwich topology with two antiparallel β-sheets and one short α-helix. Although the structure of PgDUF2436 was determined by the molecular-replacement method using an AlphaFold model structure as a template, there were significant differences in the positions of β1 between the AlphaFold model and the experimentally determined PgDUF2436 structure. The Basic Local Alignment Search Tool sequence-similarity search program showed no sequentially similar proteins in the Protein Data Bank. However, DaliLite search results using structure-based alignment revealed that the PgDUF2436 structure has structural similarity Z-scores of 5.9–5.4 with the C-terminal domain of AlgF, the D4 domain of cytolysin, IglE and the extracellular domain structure of PepT2. This study has elucidated the structure of the DUF2436 domain for the first time and a comparative analysis with similar structures has been performed.

The article presents a non-invasive nanoscale imaging technique that can be used in screening crystallization conditions for protein micro- and nanocrystals.

This article reports an investigation into the effects of specific radiation damage to halogenated ligands in crystal structures of protein-inhibitor complexes.

The title compound {systematic name: (2S)-2-aza­niumyl-3-[(2-carb­oxy­ethane)­sulfon­yl]propano­ate}, C6H11NO6S, forms enanti­opure crystals in the monoclinic space group P21 and exists as a zwitterion, with a protonated α-amino group and a deprotonated α-carboxyl group. Both the carboxyl groups and the amino group are involved in an extensive multicentered inter­molecular hydrogen-bonding scheme. In the crystal, the diperiodic network of hydrogen bonds propagates parallel to (101) and involves inter­connected heterodromic R43(10) rings. Electrostatic forces are major contributors to the structure energy, which was estimated by DFT calculations as Etotal = −333.5 kJ mol−1.

The technique of time-resolved macromolecular crystallography (TR-MX) has recently been rejuvenated at synchrotrons, resulting in the design of dedicated beamlines. Using pump–probe schemes, this should make the mechanistic study of photoactive proteins and other suitable systems possible with time resolutions down to microseconds. In order to identify relevant time delays, time-resolved spectroscopic experiments directly performed on protein crystals are often desirable. To this end, an instrument has been built at the icOS Lab (in crystallo Optical Spectroscopy Laboratory) at the European Synchrotron Radiation Facility using reflective focusing objectives with a tuneable nanosecond laser as a pump and a microsecond xenon flash lamp as a probe, called the TR-icOS (time-resolved icOS) setup. Using this instrument, pump–probe spectra can rapidly be recorded from single crystals with time delays ranging from a few microseconds to seconds and beyond. This can be repeated at various laser pulse energies to track the potential presence of artefacts arising from two-photon absorption, which amounts to a power titration of a photoreaction. This approach has been applied to monitor the rise and decay of the M state in the photocycle of crystallized bacteriorhodopsin and showed that the photocycle is increasingly altered with laser pulses of peak fluence greater than 100 mJ cm−2, providing experimental laser and delay parameters for a successful TR-MX experiment.

Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and polymerizes through the N-terminus, which is presented as a highly flexible arm, as demonstrated in this article. The nucleoprotein exists in an `open' or a `closed' conformation. In the case of the closed conformation the flexible N-terminal arm folds over the RNA-binding cleft, preventing RNA adsorption. In the open conformation the arm is extended in such a way that both RNA adsorption and N polymerization are possible. In this article, single-crystal X-ray diffraction and small-angle X-ray scattering were used to study the N protein of Toscana virus complexed with a single-chain camelid antibody (VHH) and it is shown that in the presence of the antibody the nucleoprotein is unable to achieve a functional assembly to form a ribonucleoprotein complex.

Macromolecular crystallography generally requires the recovery of missing phase information from diffraction data to reconstruct an electron-density map of the crystallized molecule. Most recent structures have been solved using molecular replacement as a phasing method, requiring an a priori structure that is closely related to the target protein to serve as a search model; when no such search model exists, molecular replacement is not possible. New advances in computational machine-learning methods, however, have resulted in major advances in protein structure predictions from sequence information. Methods that generate predicted structural models of sufficient accuracy provide a powerful approach to molecular replacement. Taking advantage of these advances, AlphaFold predictions were applied to enable structure determination of a bacterial protein of unknown function (UniProtKB Q63NT7, NCBI locus BPSS0212) based on diffraction data that had evaded phasing attempts using MIR and anomalous scattering methods. Using both X-ray and micro-electron (microED) diffraction data, it was possible to solve the structure of the main fragment of the protein using a predicted model of that domain as a starting point. The use of predicted structural models importantly expands the promise of electron diffraction, where structure determination relies critically on molecular replacement.

Metalloproteins are ubiquitous in all living organisms and take part in a very wide range of biological processes. For this reason, their experimental characterization is crucial to obtain improved knowledge of their structure and biological functions. The three-dimensional structure represents highly relevant information since it provides insight into the interaction between the metal ion(s) and the protein fold. Such interactions determine the chemical reactivity of the bound metal. The available PDB structures can contain errors due to experimental factors such as poor resolution and radiation damage. A lack of use of distance restraints during the refinement and validation process also impacts the structure quality. Here, the aim was to obtain a thorough overview of the distribution of the distances between metal ions and their donor atoms through the statistical analysis of a data set based on more than 115 000 metal-binding sites in proteins. This analysis not only produced reference data that can be used by experimentalists to support the structure-determination process, for example as refinement restraints, but also resulted in an improved insight into how protein coordination occurs for different metals and the nature of their binding interactions. In particular, the features of carboxylate coordination were inspected, which is the only type of interaction that is commonly present for nearly all metals.

When solving a structure of a protein from single-wavelength anomalous diffraction X-ray data, the initial phases obtained by phasing from an anomalously scattering substructure usually need to be improved by an iterated electron-density modification. In this manuscript, the use of convolutional neural networks (CNNs) for segmentation of the initial experimental phasing electron-density maps is proposed. The results reported demonstrate that a CNN with U-net architecture, trained on several thousands of electron-density maps generated mainly using X-ray data from the Protein Data Bank in a supervised learning, can improve current density-modification methods.

Tryptophan is the most prominent amino acid found in proteins, with multiple functional roles. Its side chain is made up of the hydrophobic indole moiety, with two groups that act as donors in hydrogen bonds: the Nɛ—H group, which is a potent donor in canonical hydrogen bonds, and a polarized Cδ1—H group, which is capable of forming weaker, noncanonical hydrogen bonds. Due to adjacent electron-withdrawing moieties, C—H⋯O hydrogen bonds are ubiquitous in macromolecules, albeit contingent on the polarization of the donor C—H group. Consequently, Cα—H groups (adjacent to the carbonyl and amino groups of flanking peptide bonds), as well as the Cɛ1—H and Cδ2—H groups of histidines (adjacent to imidazole N atoms), are known to serve as donors in hydrogen bonds, for example stabilizing parallel and antiparallel β-sheets. However, the nature and the functional role of interactions involving the Cδ1—H group of the indole ring of tryptophan are not well characterized. Here, data mining of high-resolution (r ≤ 1.5 Å) crystal structures from the Protein Data Bank was performed and ubiquitous close contacts between the Cδ1—H groups of tryptophan and a range of electronegative acceptors were identified, specifically main-chain carbonyl O atoms immediately upstream and downstream in the polypeptide chain. The stereochemical analysis shows that most of the interactions bear all of the hallmarks of proper hydrogen bonds. At the same time, their cohesive nature is confirmed by quantum-chemical calculations, which reveal interaction energies of 1.5–3.0 kcal mol−1, depending on the specific stereochemistry.