Abstract
Steady progress has been made in the field of ab initio protein folding. A variety of methods now allow the prediction of low-resolution structures of small proteins or protein fragments up to approximately 100 amino acid residues in length. Such low-resolution structures may be sufficient for the functional annotation of protein sequences on a genome-wide scale. Although no consistently reliable algorithm is currently available, the essential challenges to developing a general theory or approach to protein structure prediction are better understood. The energy landscapes resulting from the structure prediction algorithms are only partially funneled to the native state of the protein. This review focuses on two areas of recent advances in abinitio structure prediction - improvements in the energy functions and strategies to search the caldera region of the energy landscapes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 176-181 |
| Number of pages | 6 |
| Journal | Current Opinion in Structural Biology |
| Volume | 12 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 1 2002 |
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ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
Cite this
Ab initio protein structure prediction. / Hardin, Corey; Pogorelov, Taras V; Luthey-Schulten, Zaida Ann.
In: Current Opinion in Structural Biology, Vol. 12, No. 2, 01.04.2002, p. 176-181.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Ab initio protein structure prediction
AU - Hardin, Corey
AU - Pogorelov, Taras V
AU - Luthey-Schulten, Zaida Ann
PY - 2002/4/1
Y1 - 2002/4/1
N2 - Steady progress has been made in the field of ab initio protein folding. A variety of methods now allow the prediction of low-resolution structures of small proteins or protein fragments up to approximately 100 amino acid residues in length. Such low-resolution structures may be sufficient for the functional annotation of protein sequences on a genome-wide scale. Although no consistently reliable algorithm is currently available, the essential challenges to developing a general theory or approach to protein structure prediction are better understood. The energy landscapes resulting from the structure prediction algorithms are only partially funneled to the native state of the protein. This review focuses on two areas of recent advances in abinitio structure prediction - improvements in the energy functions and strategies to search the caldera region of the energy landscapes.
AB - Steady progress has been made in the field of ab initio protein folding. A variety of methods now allow the prediction of low-resolution structures of small proteins or protein fragments up to approximately 100 amino acid residues in length. Such low-resolution structures may be sufficient for the functional annotation of protein sequences on a genome-wide scale. Although no consistently reliable algorithm is currently available, the essential challenges to developing a general theory or approach to protein structure prediction are better understood. The energy landscapes resulting from the structure prediction algorithms are only partially funneled to the native state of the protein. This review focuses on two areas of recent advances in abinitio structure prediction - improvements in the energy functions and strategies to search the caldera region of the energy landscapes.
UR - http://www.scopus.com/inward/record.url?scp=0036535974&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036535974&partnerID=8YFLogxK
U2 - 10.1016/S0959-440X(02)00306-8
DO - 10.1016/S0959-440X(02)00306-8
M3 - Review article
C2 - 11959494
AN - SCOPUS:0036535974
VL - 12
SP - 176
EP - 181
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
SN - 0959-440X
IS - 2
ER -