Results 291 to 300 of about 3,699,805 (346)
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Current Opinion in Chemical Biology, 2001
The prediction of protein structure, based primarily on sequence and structure homology, has become an increasingly important activity. Homology models have become more accurate and their range of applicability has increased. Progress has come, in part, from the flood of sequence and structure information that has appeared over the past few years, and ...
B, Al-Lazikani +3 more
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The prediction of protein structure, based primarily on sequence and structure homology, has become an increasingly important activity. Homology models have become more accurate and their range of applicability has increased. Progress has come, in part, from the flood of sequence and structure information that has appeared over the past few years, and ...
B, Al-Lazikani +3 more
openaire +2 more sources
Current Opinion in Biotechnology, 1998
Genome sequencing projects continue to provide a flood of new protein sequences, and prediction methods remain an important means of adding structural information. Recently, there have been advances in secondary structure prediction, which feed, in turn, into improved fold recognition algorithms.
D R, Westhead, J M, Thornton
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Genome sequencing projects continue to provide a flood of new protein sequences, and prediction methods remain an important means of adding structural information. Recently, there have been advances in secondary structure prediction, which feed, in turn, into improved fold recognition algorithms.
D R, Westhead, J M, Thornton
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Science, 1996
Elizabeth Pennisi's Research News article “Teams tackle protein prediction” ([26 July, p. 426][1]) describes an ongoing project, known as CASP (for Critical Assessment of Techniques for Protein Structure Prediction) ([1][2]), to provide researchers who model protein structures with the opportunity to jointly make bona fide predictions, announced before
S A, Benner, D L, Geroff, J D, Rozzell
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Elizabeth Pennisi's Research News article “Teams tackle protein prediction” ([26 July, p. 426][1]) describes an ongoing project, known as CASP (for Critical Assessment of Techniques for Protein Structure Prediction) ([1][2]), to provide researchers who model protein structures with the opportunity to jointly make bona fide predictions, announced before
S A, Benner, D L, Geroff, J D, Rozzell
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2008
Protein structure prediction has matured over the past few years to the point that even fully automated methods can provide reasonably accurate three-dimensional models of protein structures. However, until now it has not been possible to develop programs able to perform as well as human experts, who are still capable of systematically producing better
AlLazikani B, Hill EE, Morea V
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Protein structure prediction has matured over the past few years to the point that even fully automated methods can provide reasonably accurate three-dimensional models of protein structures. However, until now it has not been possible to develop programs able to perform as well as human experts, who are still capable of systematically producing better
AlLazikani B, Hill EE, Morea V
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Deconstructing protein structure
Current Biology, 1991Proteins are responsible for many important cellular functions, and in order to fulfrtl its role, each protein must fold correctly into a unique three-dimensional structure. Three decades of research on a wide variety of proteins have confirmed Anfinsen’s originaI demonstration that the primary ammo acid sequence encodes all the information necessary ...
S, Marqusee, L, Regan
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Journal of Biomolecular Structure and Dynamics, 2003
Recent sequence analysis of complete prokaryotic proteomes suggests that in early evolutionary stages proteins were rather small, of the size 25-35 amino acids. Corroborating evidence comes from protein crystal data, which indicate this size for closed loops--universal structural units of globular proteins.
Igor N, Berezovsky +3 more
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Recent sequence analysis of complete prokaryotic proteomes suggests that in early evolutionary stages proteins were rather small, of the size 25-35 amino acids. Corroborating evidence comes from protein crystal data, which indicate this size for closed loops--universal structural units of globular proteins.
Igor N, Berezovsky +3 more
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Acta Crystallographica Section D Biological Crystallography, 2002
The Protein Data Bank (PDB) is the primary source of macromolecular structure data for a worldwide community of users. A subset of those users then process these data to derive secondary information which is also available on the WWW. This process includes validation, some form of reductionism, via sequence or structure, or visualization. The result, a
Helge, Weissig, Philip E, Bourne
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The Protein Data Bank (PDB) is the primary source of macromolecular structure data for a worldwide community of users. A subset of those users then process these data to derive secondary information which is also available on the WWW. This process includes validation, some form of reductionism, via sequence or structure, or visualization. The result, a
Helge, Weissig, Philip E, Bourne
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Molecular Biotechnology, 2009
Web-based protein structure databases come in a wide variety of types and levels of information content. Those having the most general interest are the various atlases that describe each experimentally determined protein structure and provide useful links, analyses, and schematic diagrams relating to its 3D structure and biological function.
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Web-based protein structure databases come in a wide variety of types and levels of information content. Those having the most general interest are the various atlases that describe each experimentally determined protein structure and provide useful links, analyses, and schematic diagrams relating to its 3D structure and biological function.
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2010
The tertiary structure of proteins can reveal information that is hard to detect in a linear sequence. Knowing the tertiary structure is valuable when generating hypothesis and interpreting data. Unfortunately, the gap between the number of known protein sequences and their associated structures is widening.
Lars, Malmström, David R, Goodlett
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The tertiary structure of proteins can reveal information that is hard to detect in a linear sequence. Knowing the tertiary structure is valuable when generating hypothesis and interpreting data. Unfortunately, the gap between the number of known protein sequences and their associated structures is widening.
Lars, Malmström, David R, Goodlett
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Encephalitogenic Protein: Structure
Science, 1969Amino acid sequences of encephalitogenic proteins from bovine cord and rabbit brain are reported. The bovine protein contains 45 residues. The rabbit protein is identical except for two isopolar substitutions, a dipeptide and amino acid deletion. Analysis of this protein and a 140-residue myelin basic protein indicates that the smaller protein is a ...
R F, Kibler +5 more
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