Kraig Biocraft Laboratories Inc (KBLB)

[TRUISM]

SPIBER HAS ACADEMIC PAPERS ON THEIR WEBSITE.

Feel free to peruse at your earliest convenience:

Spiber's Academic Research On Structural Proteins


INTRODUCTION


The methods and technologies Spiber has developed for the production and utilization of our materials are based on a multitude of interdisciplinary research initiatives. Many important questions crucial to structural protein development and production remain unanswered, particularly in the frontier research topic that forms Spiber’s core competency—understanding the mechanism that drives the expression of our specially-designed proteins.

We believe that pioneering the new technologies and knowledge required by our endeavour will require a coordinated fusion of the best solutions that academia and industry have to offer.

By applying the latest academic developments to the cyclical research and development process that drives our efforts to commercialize structural proteins, we believe that we can contribute to the global scientific endeavor to bring about a more sustainable future. It is this belief that inspires our research into a wide range of natural protein materials and their properties, from the incredible softness of premium luxury cashmere to the tough and tensile spider silk that inspired our company’s name.

Protein materials are unmatched in terms of their potential for diversity across both form and function, and we are confident that their impact on humanity and the world will only continue to grow as our knowledge and ability to utilize them increases through the combined efforts of industry and academia.

International Journal of Biological Macromolecules



February 23, 2022
The solubility of N-acetyl amino acid amides in organic acid and alcohol solutions: Mechanistic insight into structural protein solubilization
Atsushi Hirano, Momoyo Wada, Takehiro K.Sato, Tomoshi Kameda
-> Abstract
Molecules
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January 14, 2022
Presence of ß-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR
Yu Suzuki, Takanori Higash, Takahiro Yamamoto, Hideyasu Okamura, Takehiro K. Sato and Tetsuo Asakura
-> Abstract
Open Biology
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December 22, 2021
Darwin’s bark spider shares a spidroin repertoire with Caerostris extrusa but achieves extraordinary silk toughness through gene expression
Nobuaki Kono, Rintaro Ohtoshi, Ali D. Malay, Masaru Mori, Hiroyasu Masunaga, Yuki Yoshida, Hiroyuki Nakamura, Keiji Numata and Kazuharu Arakawa
-> Abstract
Engineering Biology
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December 10, 2021
Fuelling the future of sustainable sugar fermentation across generations
David Lips
-> Abstract
Data in Brief
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September 20, 2021
Transcriptomic data during development of a two-spotted cricket Gryllus bimaculatus
Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Kazuharu Arakawa
-> Abstract
Perspective | Emerging Topics in Life Sciences
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September 08, 2021
Practical considerations for delivering on the sustainability promise of fermentation-based biomanufacturing
David Lips
-> Abstract
Proceedings of the National Academy of Science of the United States of America
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August 06, 2021
Multicomponent nature underlies the extraordinary mechanical properties of spider dragline silk
Nobuaki Kono, Hiroyuki Nakamura, Masaru Mori, Yuki Yoshida, Rintaro Ohtoshi, Ali D. Malay, Daniel A. Pedrazzoli Moran, Masaru Tomita, Keiji Numata, and Kazuharu Arakawa
-> Abstract
Zoological Letters
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July 26, 2021
The balance of crystalline and amorphous regions in the fibroin structure underpins the tensile strength of bagworm silk
Nobuaki Kono, Hiroyuki Nakamura, Ayaka Tateishi, Keiji Numata and Kazuharu Arakawa
-> Abstract
Mitochondrial DNA Part B
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July 26, 2021
The complete mitochondrial genome of Trichonephila clavipes (Araneae: Araneidae)
Nobuaki Kono, Hiroyuki Nakamura and Kazuharu Arakawa
-> Abstract
Biomolecules
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April 12, 2021
Xanthurenic Acid Is the Main Pigment of Trichonephila clavata Gold Dragline Silk
Masayuki Fujiwara, Nobuaki Kono, Akiyoshi Hirayama, Ali D. Malay, Hiroyuki Nakamura, Rintaro Ohtoshi, Keiji Numata, Masaru Tomita and Kazuharu Arakawa
-> Abstract
Scientific Reports
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January 08, 2021
Environmental biodegradability of recombinant structural protein
Yuya Tachibana, Sunita Darbe, Senri Hayashi, Alina Kudasheva, Haruna Misawa, Yuka Shibata & Ken-ichi Kasuya
-> Abstract
Polymer Journal
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October 01, 2020
Aqueous spinning system with a citrate buffer for highly extensible silk fibers
Jianming Chen, Yoshinori Ohta, Hiroyuki Nakamura, Hiroyasu Masunaga, Keiji Numata
-> Abstract
Scientific Reports
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September 24, 2020
Spidroin profiling of cribellate spiders provides insight into the evolution of spider prey capture strategies
Nobuaki Kono, Hiroyuki Nakamura, Masaru Mori, Masaru Tomita & Kazuharu Arakawa
-> Abstract
Molecular Biology and Evolution
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August 14, 2019
Sequenceserver: a modern graphical user interface for custom BLAST databases
Anurag Priyam, Ben J Woodcroft, Vivek Rai, Ismail Moghul, Alekhya Munagala, Filip Ter, Hiten Chowdhary, Iwo Pieniak, Lawrence J Maynard, Mark Anthony Gibbins, HongKee Moon, Austin Davis-Richardson, Mahmut Uludag, Nathan S Watson-Haigh, Richard Challis, Hiroyuki Nakamura, Emeline Favreau, Esteban A Gómez, Tomás Pluskal, Guy Leonard, Wolfgang Rumpf, Yannick Wurm
-> Abstract
Scientific Reports
|
June 10, 2019
Orb-weaving spider Araneus ventricosus genome elucidates the spidroin gene catalogue
Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Daniel A. Pedrazzoli Moran, Asaka Shinohara, Yuki Yoshida, Masayuki Fujiwara, Masaru Mori, Masaru Tomita & Kazuharu Arakawa
-> Abstract
Communications Biology
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April 29, 2019
The bagworm genome reveals a unique fibroin gene that provides high tensile strength
Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Masaru Tomita, Keiji Numata & Kazuharu Arakawa
-> Abstract
Mitochondrial DNA Part B
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August 01, 2018
The complete mitochondrial genome of Eumeta variegata (Lepidoptera: Psychidae)
Kazuharu Arakawa, Nobuaki Kono, Rintaro Ohtoshi, Hiroyuki Nakamura, Masaru Tomita
-> Abstract
Polymer Degradation and Stability
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April 12, 2018
Stabilization of recombinant spider silk in thermo-oxidative degradation: High-throughput screening for antioxidants
Anh T.N. Dao, Jun'ichi Shimokata, Kengo Takeuchi, Koyuru Nakayama, Toshiaki Taniike
-> Abstract
Scientific Reports
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January 29, 2018
Reconstruction of cysteine biosynthesis using engineered cysteine-free enzymes
Kosuke Fujishima, Kendrick M. Wang, Jesse A. Palmer, Nozomi Abe, Kenji Nakahigashi, Drew Endy & Lynn J. Rothschild
-> Abstract
Macromolecules
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October 13, 2017
NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States
Yugo Tasei, Akio Nishimura, Yu Suzuki, Takehiro K. Sato, Junichi Sugahara, and Tetsuo Asakura
-> Abstract
Polymer Degradation and Stability
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August 12, 2017
Chemiluminescence from recombinant spider silk under thermo-oxidative degradation
Koyuru Nakayama, Anh T.N. Dao, Kengo Takeuchi, Junichi Shimokata, Toshiaki Taniike
-> Abstract
Polymer Chemistry
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January 02, 2017
Multilateral characterization of recombinant spider silk in thermal degradation
Anh T. N. Dao, K. Nakayama, J. Shimokata and T. Taniike
-> Abstract
Biomacromolecules
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February 02, 2016
Influence of Water Content on the ß-Sheet Formation, Thermal Stability, Water Removal, and Mechanical Properties of Silk Materials
Kenjiro Yazawa, Kana Ishida, Hiroyasu Masunaga, Takaaki Hikima and Keiji Numata
-> Abstract
Molecular Ecology Resources
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November 12, 2015
Evaluation of the impact of RNA preservation methods of spiders for de novo transcriptome assembly
Nobuaki Kono, Hiroyuki Nakamura, Yusuke Ito, Masaru Tomita, Kazuharu Arakawa
-> Abstract
Polymer
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October 23, 2015
Crystal structure and physical properties of Antheraea yamamai silk fibers: Long poly(alanine) sequences are partially in the crystalline region
Keiji Numata, Ryota Sato, Kenjiro Yazawa, Takaaki Hikima, Hiroyasu Masunaga
-> Abstract
Soft Matter
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June 30, 2015
Use of extension-deformation-based crystallisation of silk fibres to differentiate their functions in nature
Keiji Numata, Hiroyasu Masunaga, Takaaki Hikima, Sono Sasaki, Kazuhide Sekiyama and Masaki Takata
-> Abstract


IN RESPONSE TO:

Proteins are made from long chains of amino acids that may have been modified during protein formation. There are only 20 normal amino acids in most proteins. At an atomic level, lots of carbon atoms, oxygen, nitrogen, and hydrogen being the most common.

To say that something is ‘molecularly identical’ means each of these amino acids appears in the same position in the larger protein structure. Companies are now synthesizing whey protein from cow milk. It is the same protein.

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