LEADER 00000cam a2200685Ia 4500
001 ocn319518110
003 OCoLC
005 20160527041334.6
006 m o d
007 cr cn|||||||||
008 090428s2008 enka ob 001 0 eng d
019 236108497|a506334567|a671957812
020 9781847558268|q(electronic book)
020 1847558267|q(electronic book)
020 0854042725|q(hardback)
020 9780854042722|q(hardback)
020 |z1847558267
020 |z9780854042722
035 (OCoLC)319518110|z(OCoLC)236108497|z(OCoLC)506334567
|z(OCoLC)671957812
037 T2408|bRoyal Society of Chemistry|nhttp://www.rsc.org/spr
040 UKRSC|beng|epn|cUKRSC|dUKRSC|dOKU|dCUS|dN$T|dE7B|dOCLCF
|dCOO|dYDXCP|dDEBSZ|dCBT|dU5D|dOCLCQ
049 RIDW
050 4 QP624.75.P74|bP76 2008
072 7 SCI|x029000|2bisacsh
072 7 PSB|2bicssc
072 7 PNT|2bicssc
072 7 PSD|2bicssc
072 7 SCI|2eflch
082 04 572.86|222
090 QP624.75.P74|bP76 2008
245 00 Protein-nucleic acid interactions :|bstructural biology /
|cedited by Phoebe A. Rice and Carl C. Correll.
264 1 Cambridge :|bRoyal Society of Chemistry,|c[2008]
264 4 |c©2008
300 1 online resource (xvii, 397 pages) :|billustrations (some
color).
336 text|btxt|2rdacontent
337 computer|bc|2rdamedia
338 volume|bnc|2rdacarrier
340 |gpolychrome|2rdacc
347 text file|2rdaft
490 1 RSC biomolecular sciences
504 Includes bibliographical references and index.
505 0 Introduction / Carl C. Correll and Phoebe A. Rice -- Role
of water and effects of small ions in site-specific
protein-DNA interactions / Linda Jen-Jacobson and Lewis A.
Jacobson -- Structural basis for sequence-specific DNA
recognition by transcription factors and their complexes /
Manqing Hong and Ronen Marmorstein -- Indirect readout of
DNA sequence by proteins / Catherine L. Lawson and Helen
M. Berman -- Single-stranded nucleic acid (SSNA)-binding
proteins / Martin P. Horvath -- DNA junctions and their
interaction with resolving enzymes / David M.J. Lilley --
RNA-protein interactions in ribonucleoprotein particles
and ribonucleases / Hong Li -- Bending and compaction of
DNA by proteins / Reid C. Johnson, Stefano Stella and John
K. Heiss -- Mode of action of proteins with RNA chaperone
activity / Sabine Stampfl [and others] -- Structure and
function of DNA topoisomerases / Ken C. Dong and James M.
Berger -- DNA transposases / Fred Dyda and Alison Burgess
Hickman -- Site-specific recombinases / Gregory D. Van
Duyne -- DNA nucleases / Nancy C. Horton -- RNA-modifying
enzymes / Adrian R. Ferré-D'amaré.
520 Written by a team of experts, this book bridges the gap
between the DNA- and RNA- views of protein-nucleic acid
recognition which are often treated as separate fields.
|bThe structural biology of protein-nucleic acid
interactions is in some ways a mature field and in others
in its infancy. High-resolution structures of protein-DNA
complexes have been studied since the mid 1980s and a vast
array of such structures has now been determined, but
surprising and novel structures still appear quite
frequently. High-resolution structures of protein-RNA
complexes were relatively rare until the last decade.
Propelled by advances in technology as well as the
realization of RNA's importance to biology, the number of
example structures has ballooned in recent years. New
insights are now being gained from comparative studies
only recently made possible due to the size of the
database, as well as from careful biochemical and
biophysical studies. As a result of the explosion of
research in this area, it is no longer possible to write a
comprehensive review. Instead, current review articles
tend to focus on particular subtopics of interest. This
makes it difficult for newcomers to the field to attain a
solid understanding of the basics. One goal of this book
is therefore to provide in-depth discussions of the
fundamental principles of protein-nucleic acid
interactions as well as to illustrate those fundamentals
with up-to-date and fascinating examples for those who
already possess some familiarity with the field. The book
also aims to bridge the gap between the DNA- and the RNA-
views of nucleic acid - protein recognition, which are
often treated as separate fields. However, this is a false
dichotomy because protein - DNA and protein - RNA
interactions share many general principles. This book
therefore includes relevant examples from both sides, and
frames discussions of the fundamentals in terms that are
relevant to both. The monograph approaches the study of
protein-nucleic acid interactions in two distinctive ways.
First, DNA-protein and RNA-protein interactions are
presented together. Second, the first half of the book
develops the principles of protein-nucleic acid
recognition, whereas the second half applies these to more
specialized topics. Both halves are illustrated with
important real life examples. The first half of the book
develops fundamental principles necessary to understand
function. An introductory chapter by the editors reviews
the basics of nucleic acid structure. Jen-Jacobsen and
Jacobsen discuss how solvent interactions play an
important role in recognition, illustrated with extensive
thermodynamic data on restriction enzymes. Marmorstein and
Hong introduce the zoology of the DNA binding domains
found in transcription factors, and describe the
combinational recognition strategies used by many
multiprotein eukaryotic complexes. Two chapters discuss
indirect readout of DNA sequence in detail: Berman and
Lawson explain the basic principles and illustrate them
with in-depth studies of CAP, while in their chapter on
DNA bending and compaction Johnson, Stella and Heiss
highlight the intrinsic connections between DNA bending
and indirect readout. Horvath lays out the fundamentals of
protein recognition of single stranded DNA and single
stranded RNA, and describes how they apply in a detailed
analysis of telomere end binding proteins. Nucleic acids
adopt more complex structures - Lilley describes the
conformational properties of helical junctions, and how
proteins recognize and cleave them. Because RNA readily
folds due to the stabilizing role of its 2'-hydroxyl
groups, Li discusses how proteins recognize different RNA
folds, which include duplex RNA. With the fundamentals
laid out, discussion turns to more specialized examples
taken from important aspects of nucleic acid metabolism.
Schroeder discusses how proteins chaperone RNA by
rearranging its structure into a functional form. Berger
and Dong discuss how topoisomerases alter the topology of
DNA and relieve the superhelical tension introduced by
other processes such as replication and transcription.
Dyda and Hickman show how DNA transposes mediate genetic
mobility and Van Duyne discusses how site-specific
recombinases "cut" and "paste" DNA. Horton presents a
comprehensive review of the structural families and
chemical mechanisms of DNA nucleases, whereas Li in her
discussion of RNA-protein recognition also covers RNA
nucleases. Lastly, Ferre-D'Amare shows how proteins
recognize and modify RNA transcripts at specific sites.
The book also emphasises the impact of structural biology
on understanding how proteins interact with nucleic acids
and it is intended for advanced students and established
scientists wishing to broaden their horizons.
590 eBooks on EBSCOhost|bEBSCO eBook Subscription Academic
Collection - North America
650 0 DNA-protein interactions.|0https://id.loc.gov/authorities/
subjects/sh91001921
650 0 RNA-protein interactions.|0https://id.loc.gov/authorities/
subjects/sh92005077
650 7 DNA-protein interactions.|2fast|0https://id.worldcat.org/
fast/886616
650 7 RNA-protein interactions.|2fast|0https://id.worldcat.org/
fast/1086260
655 4 Electronic books.
700 1 Rice, Phoebe A.|0https://id.loc.gov/authorities/names/
nb2008010478
700 1 Correll, Carl C.|0https://id.loc.gov/authorities/names/
nb2008010479
776 08 |iPrint version:|z9780854042722|z0854042725
|w(OCoLC)212431625
830 0 RSC biomolecular sciences.|0https://id.loc.gov/authorities
/names/n2006182099
856 40 |uhttps://rider.idm.oclc.org/login?url=http://
search.ebscohost.com/login.aspx?direct=true&scope=site&
db=nlebk&AN=496358|zOnline eBook. Access restricted to
current Rider University students, faculty, and staff.
856 42 |3Instructions for reading/downloading this eBook|uhttp://
guides.rider.edu/ebooks/ebsco
901 MARCIVE 20231220
948 |d201606016|cEBSCO|tebscoebooksacademic|lridw
994 92|bRID
