Results 51 to 60 of about 2,642,890 (372)

Factors affecting sorghum protein digestibility [PDF]

, 2003
In the semi-arid tropics worldwide, sorghum (Sorghum bicolor (L.) Moench) is cultivated by farmers on a subsistence level and consumed as food by humans.
Belton, Peter, Duodu, K, Hamaker, BR, Taylor, JRN   +3 more
core   +1 more source

MAS NMR detection of hydrogen bonds for protein secondary structure characterization [PDF]

, 2020
Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen atoms and
Friedrich, Daniel, Nieuwkoop, Andrew J., Oschkinat, Hartmut, Perodeau, Jacqueline   +3 more
core   +1 more source

Continuum Secondary Structure Captures Protein Flexibility [PDF]

Structure, 2002
The DSSP program assigns protein secondary structure to one of eight states. This discrete assignment cannot describe the continuum of thermal fluctuations. Hence, a continuous assignment is proposed. Technically, the continuum results from averaging over ten discrete DSSP assignments with different hydrogen bond thresholds.
Andersen, Claus A.F., Palmer, Arthur G., Brunak, Søren, Rost, Burkhard   +3 more
openaire   +2 more sources

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill, Ansari AA, Atvinder K. Rullay, Bertozzi CR, Blanch EW, Borchelt D, Caughey B, Caughey B, Caughey B, Caughey BW, Critchley P, David H. Crout, Eberl H, Ferris A, Georges C, Gill AC, Govaerts C, Haire LF, Harris DA, Hornemann S, Ian D. Sylvester, Imanpreet K. Bath, Kazlauskaite J, Kazlauskaite J, Kenyon GL, King SA, Kirby L, Klein TR, Kocienski PJ, Legname G, Matthew R. Hicks, Mui B, Nosjean O, Pan KM, Poss AJ, Safar J, Seddon AM, Shyng SL, Stahl N, Stahl N, Teresa J. T. Pinheiro, Whitesell JK, Wuthrich K, Zahn R, Zhang ZY   +44 more
core   +1 more source

The Quality Characteristics Comparison of Stone-Milled Dried Whole Wheat Noodles, Dried Wheat Noodles, and Commercially Dried Whole Wheat Noodles

Foods, 2022
To explore the quality differences between dried wheat noodles (DWNs), stone-milled dried whole wheat noodles (SDWWNs), and commercially dried whole wheat noodles (CDWWNs), the cooking quality, texture properties, microstructure, protein secondary ...
Mengdi Cai, Chunxia Shen, Yuhui Li, Shuangli Xiong, Feng Li   +4 more
doaj   +1 more source

Sulfur-mediated chalcogen versus hydrogen bonds in proteins: a see-saw effect in the conformational space

QRB Discovery, 2023
Divalent sulfur (S) forms a chalcogen bond (Ch-bond) via its σ-holes and a hydrogen bond (H-bond) via its lone pairs. The relevance of these interactions and their interplay for protein structure and function is unclear.
Vishal Annasaheb Adhav, Sanket Satish Shelke, Pananghat Balanarayan, Kayarat Saikrishnan   +3 more
doaj   +1 more source

SSEP: secondary structural elements of proteins [PDF]

Nucleic Acids Research, 2003
SSEP is a comprehensive resource for accessing information related to the secondary structural elements present in the 25 and 90% non-redundant protein chains. The database contains 1771 protein chains from 1670 protein structures and 6182 protein chains from 5425 protein structures in 25 and 90% non-redundant protein chains, respectively.
Shanthi, V, Selvarani, P, Kumar, Kiran Ch, Mohire, CS, Sekar, K   +4 more
openaire   +2 more sources

Recoverable One-dimensional Encoding of Three-dimensional Protein Structures

, 2005
Protein one-dimensional (1D) structures such as secondary structure and contact number provide intuitive pictures to understand how the native three-dimensional (3D) structure of a protein is encoded in the amino acid sequence.
A. R. Kinjo, Berman, Havel, K. Nishikawa, Kabsch, Kinjo, Nakai, Plaxco, Porto, Vendruscolo, Wang   +10 more
core   +2 more sources

Identification of a protein encoded in the EB-viral open reading frame BMRF2 [PDF]

, 1992
Using monospecific rabbit sera against a peptide derived from a potential antigenic region of the Epstein-Barr viral amino acid sequence encoded in the open reading frame BMRF2 we could identify a protein-complex of 53/55 kDa in chemically induced B95-8,
A. v. Brunn, B Böttinger, E Tschachler, G Myers, GJ Clements, GJ LaRosa, H Takahashi, H Takahashi, H Takahashi, H. Fließbach, H. Wolf, HK Lyerly, HK Lyerly, J Goudsmit, J Goudsmit, JE Gregersen, K Javaherian, K Javaherian, LA Lasky, M Clerici, M Clerici, M. Niedrig, NL Haigwood, P Simmonds, PJ Durda, PW Berman, R Wagner, R. Wagner, RA Neurath, RH Meloen, S Modrow, S Modrow, SD Putney, Susanne Modrow, T Hattori, TJ Palker, Traudel Böltz, Y Devash   +37 more
core   +2 more sources

TMPSS: A Deep Learning-Based Predictor for Secondary Structure and Topology Structure Prediction of Alpha-Helical Transmembrane Proteins

Frontiers in Bioengineering and Biotechnology, 2021
Alpha transmembrane proteins (αTMPs) profoundly affect many critical biological processes and are major drug targets due to their pivotal protein functions.
Zhe Liu, Zhe Liu, Yingli Gong, Yihang Bao, Yuanzhao Guo, Han Wang, Guan Ning Lin, Guan Ning Lin   +7 more
doaj   +1 more source